NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2023447759|gb|QTQ13545|]
View 

M23 family metallopeptidase [Treponema parvum]

Protein Classification

LysM and M23_peptidase domain-containing protein( domain architecture ID 11443402)

LysM and M23_peptidase domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 270-411 2.56e-62

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 199.43  E-value: 2.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 270 AKLSSDAIRLAMGEMFIYPLKGkwRRTSLFGFRSDPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIII 349
Cdd:COG0739    56 AAAAAAAAAAIALGSGAWPVKG--RITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVII 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023447759 350 NHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTVLK 411
Cdd:COG0739   134 DHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
100-270 1.10e-13

LysM repeat [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.20  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 100 PYAVKIASSYLSSFANPLVLEDVPAEELEILNKIMADFALERSNEFDENGDVLNADGFSASPSEINFRQPVSYRTYVVQS 179
Cdd:COG1388    11 ALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 180 GDTILGITRRFGLSNISTLIavndianvrrlrfgqklvvpsmdglVHTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNL 259
Cdd:COG1388    91 GDTLSGIARRYGAAAAPSPV-------------------------TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTI 145

                         170
                  ....*....|.
gi 2023447759 260 LIGAKLFIPGA 270
Cdd:COG1388   146 RPGQKLKIPAS 156
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 270-411 2.56e-62

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 199.43  E-value: 2.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 270 AKLSSDAIRLAMGEMFIYPLKGkwRRTSLFGFRSDPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIII 349
Cdd:COG0739    56 AAAAAAAAAAIALGSGAWPVKG--RITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVII 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023447759 350 NHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTVLK 411
Cdd:COG0739   134 DHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 311-406 6.49e-48

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 158.48  E-value: 6.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 311 SFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTG 390
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 2023447759 391 PHLHFTVYKNGKLVDP 406
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 313-397 1.69e-42

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 143.89  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 313 HTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTGPH 392
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 2023447759 393 LHFTV 397
Cdd:cd12797    81 LHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 287-409 2.05e-30

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 121.31  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 287 YPLKGKWRRTSLFG-FRSDPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRS 365
Cdd:PRK11649  286 FPTAKQFRISSNFNpRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKL 365

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2023447759 366 LAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTV 409
Cdd:PRK11649  366 LVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTA 409
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
100-270 1.10e-13

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.20  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 100 PYAVKIASSYLSSFANPLVLEDVPAEELEILNKIMADFALERSNEFDENGDVLNADGFSASPSEINFRQPVSYRTYVVQS 179
Cdd:COG1388    11 ALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 180 GDTILGITRRFGLSNISTLIavndianvrrlrfgqklvvpsmdglVHTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNL 259
Cdd:COG1388    91 GDTLSGIARRYGAAAAPSPV-------------------------TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTI 145

                         170
                  ....*....|.
gi 2023447759 260 LIGAKLFIPGA 270
Cdd:COG1388   146 RPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 226-268 7.88e-11

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 56.64  E-value: 7.88e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2023447759 226 HTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNLLIGAKLFIP 268
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 173-218 5.15e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 51.72  E-value: 5.15e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2023447759 173 RTYVVQSGDTILGITRRFGLSnISTLIAVNDIANVRRLRFGQKLVV 218
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVT-VEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
226-267 3.74e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 48.98  E-value: 3.74e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2023447759  226 HTVKPGDSLNALSVQYHVPVEDLLDVN-DLESHNLLIGAKLFI 267
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 169-265 5.33e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 51.66  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 169 PVSYRTYVVQSGDTILGITRRFGLSnISTLIAVNDIANvRRLRFGQKLVVPSM----------DGLVHTVKPGDSLNALS 238
Cdd:PRK10783  340 PLNSRSYKVRSGDTLSGIASRLNVS-TKDLQQWNNLRG-SKLKVGQTLTIGAGssaqrlannsDSITYRVRKGDSLSSIA 417

                          90       100
                  ....*....|....*....|....*..
gi 2023447759 239 VQYHVPVEDLLDVNDLESHNLLIGAKL 265
Cdd:PRK10783  418 KRHGVNIKDVMRWNSDTAKNLQPGDKL 444
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 270-411 2.56e-62

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 199.43  E-value: 2.56e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 270 AKLSSDAIRLAMGEMFIYPLKGkwRRTSLFGFRSDPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIII 349
Cdd:COG0739    56 AAAAAAAAAAIALGSGAWPVKG--RITSGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVII 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023447759 350 NHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTVLK 411
Cdd:COG0739   134 DHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 311-406 6.49e-48

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 158.48  E-value: 6.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 311 SFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTG 390
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 2023447759 391 PHLHFTVYKNGKLVDP 406
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 313-397 1.69e-42

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 143.89  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 313 HTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTGPH 392
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                  ....*
gi 2023447759 393 LHFTV 397
Cdd:cd12797    81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 285-411 2.23e-42

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 147.87  E-value: 2.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 285 FIYPLKGKwrRTSLFG--FRSDPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHL 362
Cdd:COG5821    69 FLKPVSGK--ITREFGedLVYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANL 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2023447759 363 -SRSLAKTGDRIDQGEKIGLVGSTG---YSTGPHLHFTVYKNGKLVDPLTVLK 411
Cdd:COG5821   147 dSKIKVKVGQKVKKGQVIGKVGSTAlfeSSEGPHLHFEVLKNGKPVDPMKYLK 199
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 285-411 6.00e-37

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 138.36  E-value: 6.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 285 FIYPLKGkwRRTSLFGFRsdpfTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSR 364
Cdd:COG4942   255 LPWPVSG--RVVRRFGER----DGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSS 328

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2023447759 365 SLAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTVLK 411
Cdd:COG4942   329 LLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLA 375
PRK11649 PRK11649
putative peptidase; Provisional
 287-409 2.05e-30

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 121.31  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 287 YPLKGKWRRTSLFG-FRSDPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRS 365
Cdd:PRK11649  286 FPTAKQFRISSNFNpRRLNPVTGRVAPHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKL 365

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2023447759 366 LAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTV 409
Cdd:PRK11649  366 LVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPLTA 409
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 305-411 9.71e-17

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 78.49  E-value: 9.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 305 PFTG--VRSF---HTGLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKI 379
Cdd:COG5833   107 PVSGkvVESFqenGKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKI 186

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2023447759 380 GLVGSTGYSTGpHLHFTVYKNGKLVDPLTVLK 411
Cdd:COG5833   187 GTVPATEGEEG-TFYFAIKKGGKFIDPIQVIS 217
PRK06148 PRK06148
hypothetical protein; Provisional
 282-395 2.51e-14

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 75.06  E-value: 2.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759  282 GEMFIYPLKGKWRRTslfgfrsdpftgvrsFHTGLDMAMPTGSPVYASMSGKVAAVGFTNV---YGNYIIINH----GNG 354
Cdd:PRK06148   425 DEAFTSRFIEGERRT---------------VHLGVDLFAPAGTPVYAPLAGTVRSVEIEAVplgYGGLVALEHetpgGDP 489

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2023447759  355 YQTLYAHLSRSLA---KTGDRIDQGEKIGLVGSTGYSTG--PHLHF 395
Cdd:PRK06148   490 FYTLYGHLAHEAVsrlKPGDRLAAGELFGAMGDAHENGGwaPHLHF 535
nlpD PRK10871
murein hydrolase activator NlpD;
304-410 7.69e-14

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 71.79  E-value: 7.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 304 DPFTGVRSFHTGLDMAMPTGSPVYASMSGKVAAVGftNV---YGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKIG 380
Cdd:PRK10871  210 ENFSASEGGNKGIDIAGSKGQAIIATADGRVVYAG--NAlrgYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIA 287

                          90       100       110
                  ....*....|....*....|....*....|
gi 2023447759 381 LVGSTGYSTgPHLHFTVYKNGKLVDPLTVL 410
Cdd:PRK10871  288 TMGSTGTSS-TRLHFEIRYKGKSVNPLRYL 316
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
100-270 1.10e-13

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 68.20  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 100 PYAVKIASSYLSSFANPLVLEDVPAEELEILNKIMADFALERSNEFDENGDVLNADGFSASPSEINFRQPVSYRTYVVQS 179
Cdd:COG1388    11 ALLAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKS 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 180 GDTILGITRRFGLSNISTLIavndianvrrlrfgqklvvpsmdglVHTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNL 259
Cdd:COG1388    91 GDTLSGIARRYGAAAAPSPV-------------------------TYTVKKGDTLWSIARRYGVSVEELKRWNGLSSDTI 145

                         170
                  ....*....|.
gi 2023447759 260 LIGAKLFIPGA 270
Cdd:COG1388   146 RPGQKLKIPAS 156
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 226-268 7.88e-11

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 56.64  E-value: 7.88e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2023447759 226 HTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNLLIGAKLFIP 268
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 173-218 5.15e-09

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 51.72  E-value: 5.15e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2023447759 173 RTYVVQSGDTILGITRRFGLSnISTLIAVNDIANVRRLRFGQKLVV 218
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVT-VEELAAANPLINPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 225-267 2.94e-08

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 49.41  E-value: 2.94e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2023447759 225 VHTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNLL-IGAKLFI 267
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIyPGQKLKI 45
LysM smart00257
Lysin motif;
226-267 3.74e-08

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 48.98  E-value: 3.74e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2023447759  226 HTVKPGDSLNALSVQYHVPVEDLLDVN-DLESHNLLIGAKLFI 267
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNnILDPDNLQVGQKLKI 44
PRK11637 PRK11637
AmiB activator; Provisional
 315-407 7.56e-08

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 53.93  E-value: 7.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 315 GLDMAMPTGSPVYASMSGKVAAVGFTNVYGNYIIINHGNGYQTLYAHLSRSLAKTGDRIDQGEKIGLVGSTGYSTGPHLH 394
Cdd:PRK11637  331 GMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLY 410

                          90
                  ....*....|...
gi 2023447759 395 FTVYKNGKLVDPL 407
Cdd:PRK11637  411 FEIRRQGQAVNPQ 423
LysM smart00257
Lysin motif;
174-218 1.36e-07

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 47.44  E-value: 1.36e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2023447759  174 TYVVQSGDTILGITRRFGLSnISTLIAVNDIANVRRLRFGQKLVV 218
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGIS-VSDLLELNNILDPDNLQVGQKLKI 44
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 175-219 2.28e-07

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 47.01  E-value: 2.28e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2023447759 175 YVVQSGDTILGITRRFGLSnISTLIAVNDIANvRRLRFGQKLVVP 219
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGIT-VEQLAELNGLSS-PNLYVGQKLKIP 43
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 169-265 5.33e-07

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 51.66  E-value: 5.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 169 PVSYRTYVVQSGDTILGITRRFGLSnISTLIAVNDIANvRRLRFGQKLVVPSM----------DGLVHTVKPGDSLNALS 238
Cdd:PRK10783  340 PLNSRSYKVRSGDTLSGIASRLNVS-TKDLQQWNNLRG-SKLKVGQTLTIGAGssaqrlannsDSITYRVRKGDSLSSIA 417

                          90       100
                  ....*....|....*....|....*..
gi 2023447759 239 VQYHVPVEDLLDVNDLESHNLLIGAKL 265
Cdd:PRK10783  418 KRHGVNIKDVMRWNSDTAKNLQPGDKL 444
PRK13914 PRK13914
invasion associated endopeptidase;
219-276 1.66e-06

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 50.19  E-value: 1.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2023447759 219 PSMD--GLVHTVKPGDSLNALSVQYHVPVEDLLDVNDLESHNLLIGAKLFI--------PGAKLSSDA 276
Cdd:PRK13914  193 PVVDqnATTHAVKSGDTIWALSVKYGVSVQDIMSWNNLSSSSIYVGQKLAIkqtantatPKAEVKTEA 260
PRK06347 PRK06347
1,4-beta-N-acetylmuramoylhydrolase;
173-267 2.33e-05

1,4-beta-N-acetylmuramoylhydrolase;


Pssm-ID: 180536 [Multi-domain]  Cd Length: 592  Bit Score: 46.61  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 173 RTYVVQSGDTILGITRRFGLSnISTLIAVNDIANvRRLRFGQKLVV------------------PSMDGL-VHTVKPGDS 233
Cdd:PRK06347  480 KVYTVAKGDSLWRIANNNKVT-IANLKSWNNLKS-DFIYPGQKLKVsagsttnntntakpstnkPSNSTVkTYTVKKGDS 557

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2023447759 234 LNALSVQYHVPVEDLLDVNDLESHNLLIGAKLFI 267
Cdd:PRK06347  558 LWAISRQYKTTVDNIKAWNKLTSNMIHVGQKLTI 591
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 168-219 2.46e-04

Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion transport and metabolism];


Pssm-ID: 441258 [Multi-domain]  Cd Length: 163  Bit Score: 41.53  E-value: 2.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2023447759 168 QPVSYRTYVVQSGDTILGITRRF-GLSNISTLIA-VN--DIANVRRLRFGQKLVVP 219
Cdd:COG1652   105 APDAPKTYTVKPGDTLWGIAKRFyGDPARWPEIAeANrdQIKNPDLIYPGQVLRIP 160
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 173-409 2.52e-04

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 43.12  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 173 RTYVVQSGDTILGITRRFGLS--NISTLIAVNDIANV-RRLRFGQKLVVpSMD------GLVHTVKPGDSL--------- 234
Cdd:COG3061    70 QEYTVQSGDTLSQIFRRLGLSasDLYALLAAEGDAKPlSRLKPGQELRF-QLDadgqlqALRYEVSRLETLlftrqgdgf 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 235 --NALSVQYHVPVEDLLDVNDLESHNLLIGAKLFIPGAKLSSDA-IRLAMGEMFIYPLKGKW------------------ 293
Cdd:COG3061   149 qrKRVTELSDGSFSADAALASLETLELAAAAGILSDFIAAALDAgAGDAGLVELEIILDDDIdfadllfaadrftgdyfr 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023447759 294 ------------------------RRTSLFGFRSDPFTGVRSFHTGL---------DMAMPTGSPVYASMSGKVAAVGFT 340
Cdd:COG3061   229 vyaegeggdggyigaggfraakfrRRAVRFRRSSSSSSYRRRPHRLSrrrrlrrgpDAAAPSGSSNAAGGGGHKITRRGG 308

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2023447759 341 NVYGNYIIINHGNGYQTLYAHLSR--SLAKTGDRIDQGEKIGLVGSTGYSTGPHLHFTVYKNGKLVDPLTV 409
Cdd:COG3061   309 GGGGAAVGVGTGTPTTGAGLGVVRggRGGGGGVVVGQIGRGGTYGGTGLHLHKHGHKGGGVVGQGVTIGTL 379
PRK14125 PRK14125
cell division suppressor protein YneA; Provisional
 227-280 5.79e-03

cell division suppressor protein YneA; Provisional


Pssm-ID: 184523 [Multi-domain]  Cd Length: 103  Bit Score: 36.16  E-value: 5.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2023447759 227 TVKPGDSLNALSVQY----HVPVEDLL----DVNDLESHNLLIGAKLFIPGAKLSSDAIRLA 280
Cdd:PRK14125   40 TVQEGDTLWALADQYagkhHMAKNEFIewveDVNNLPSGHIKAGDKLVIPVLKSKSDSYILA 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH