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Conserved domains on  [gi|1893763502|ref|WP_185680785|]
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M23 family metallopeptidase, partial [Novosphingobium piscinae]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

EC:  3.4.24.-
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M23
PubMed:  36386627

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-340 2.13e-41

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: 148.37  E-value: 2.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 203 RFTWPAPGKVRRGFVARARGASssearsrrgapasPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGW 282
Cdd:COG4942   254 KLPWPVSGRVVRRFGERDGGGG-------------RNKGIDIAAPPGAPVRAVADGTVVYAGWLRG-YGNLVIIDHGGGY 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1893763502 283 FSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTTELHFEIRRNTVPRDPEALLPKR 340
Cdd:COG4942   320 LTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAKR 377
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
41-150 3.81e-09

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


:

Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 55.10  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502  41 PRGTEPAAESDPRTETRHVVRAGETLGGIANRAEVPriliieanalpppyavregqvlVIPRRRSHRVKEGETGFAIAMD 120
Cdd:COG1388    69 KAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAA----------------------AAPSPVTYTVKKGDTLWSIARR 126

                          90       100       110
                  ....*....|....*....|....*....|
gi 1893763502 121 YGVPWSAIAVANGIDPKgRVRAGQALVIPT 150
Cdd:COG1388   127 YGVSVEELKRWNGLSSD-TIRPGQKLKIPA 155
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-340 2.13e-41

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: 148.37  E-value: 2.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 203 RFTWPAPGKVRRGFVARARGASssearsrrgapasPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGW 282
Cdd:COG4942   254 KLPWPVSGRVVRRFGERDGGGG-------------RNKGIDIAAPPGAPVRAVADGTVVYAGWLRG-YGNLVIIDHGGGY 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1893763502 283 FSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTTELHFEIRRNTVPRDPEALLPKR 340
Cdd:COG4942   320 LTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAKR 377
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 237-333 5.55e-34

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: 120.34  E-value: 5.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 237 SPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGWFSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTS 316
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGG-YGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 1893763502 317 TTELHFEIRRNTVPRDP 333
Cdd:pfam01551  80 GPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 239-324 1.01e-31

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: 114.23  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 239 HDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGWFSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTT 318
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGG-YGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGP 79


                  ....*.
gi 1893763502 319 ELHFEI 324
Cdd:cd12797    80 HLHFEI 85
nlpD PRK10871
murein hydrolase activator NlpD;
206-340 2.57e-20

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 89.89  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 206 WPAPGKVRRGFvarargaSSSEARSRrgapasphdGIDIAGAKGDPVRAAAPGLVWYAGKEPNLYGNVVIIDHGRGWFSA 285
Cdd:PRK10871  202 WPTDGKVIENF-------SASEGGNK---------GIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 265

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1893763502 286 YAKLSKVTVKKGELVRGGERVGLIGNTGsTSTTELHFEIRRNTVPRDPEALLPKR 340
Cdd:PRK10871  266 YAHNDTMLVREQQEVKAGQKIATMGSTG-TSSTRLHFEIRYKGKSVNPLRYLPQR 319
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
41-150 3.81e-09

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 55.10  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502  41 PRGTEPAAESDPRTETRHVVRAGETLGGIANRAEVPriliieanalpppyavregqvlVIPRRRSHRVKEGETGFAIAMD 120
Cdd:COG1388    69 KAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAA----------------------AAPSPVTYTVKKGDTLWSIARR 126

                          90       100       110
                  ....*....|....*....|....*....|
gi 1893763502 121 YGVPWSAIAVANGIDPKgRVRAGQALVIPT 150
Cdd:COG1388   127 YGVSVEELKRWNGLSSD-TIRPGQKLKIPA 155
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 106-149 1.16e-08

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: 50.47  E-value: 1.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1893763502 106 HRVKEGETGFAIAMDYGVPWSAIAVANGIDPKgRVRAGQALVIP 149
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSP-NLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 104-148 2.36e-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: 2.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1893763502 104 RSHRVKEGETGFAIAMDYGVPWSAIAVANGIDPKGRVRAGQALVI 148
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM smart00257
Lysin motif;
106-148 3.48e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 43.20  E-value: 3.48e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1893763502  106 HRVKEGETGFAIAMDYGVPWSAIAVANGIDPKGRVRAGQALVI 148
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 203-340 2.13e-41

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: 148.37  E-value: 2.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 203 RFTWPAPGKVRRGFVARARGASssearsrrgapasPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGW 282
Cdd:COG4942   254 KLPWPVSGRVVRRFGERDGGGG-------------RNKGIDIAAPPGAPVRAVADGTVVYAGWLRG-YGNLVIIDHGGGY 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1893763502 283 FSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTTELHFEIRRNTVPRDPEALLPKR 340
Cdd:COG4942   320 LTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAKR 377
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 138-339 1.77e-37

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: 132.79  E-value: 1.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 138 GRVRAGQALVIPTLTRAAPLPAASPSPAADRDDDDDEARPPARPAAPATGTTTGTAAATSATSGLRFTWPAPGKVRRGFV 217
Cdd:COG0739     5 LALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 218 ARARGASSSearsrrgapASPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGWFSAYAKLSKVTVKKG 297
Cdd:COG0739    85 YRRHPVTGR---------RRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGG-YGNLVIIDHGNGYTTLYAHLSSILVKVG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1893763502 298 ELVRGGERVGLIGNTGSTSTTELHFEIRRNTVPRDPEALLPK 339
Cdd:COG0739   155 QRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFLPA 196
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 237-333 5.55e-34

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: 120.34  E-value: 5.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 237 SPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGWFSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTS 316
Cdd:pfam01551   1 RFHKGIDIAAPTGTPVYAAADGVVVFAGWLGG-YGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRST 79

                          90
                  ....*....|....*..
gi 1893763502 317 TTELHFEIRRNTVPRDP 333
Cdd:pfam01551  80 GPHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 239-324 1.01e-31

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: 114.23  E-value: 1.01e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 239 HDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGWFSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTT 318
Cdd:cd12797     1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGG-YGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGP 79


                  ....*.
gi 1893763502 319 ELHFEI 324
Cdd:cd12797    80 HLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 204-339 3.30e-31

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: 116.66  E-value: 3.30e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 204 FTWPAPGKVRRGFVARARGASSSEArsrrgapASPHDGIDIAGAKGDPVRAAAPGLVWYAGKEPnLYGNVVIIDHGRGWF 283
Cdd:COG5821    69 FLKPVSGKITREFGEDLVYSKTLNE-------WRTHTGIDIAAKEGTPVKAAADGVVVEVGKDP-KYGITVVIDHGNGIK 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 284 SAYAKL-SKVTVKKGELVRGGERVGLIGNTGSTSTTE---LHFEIRRNTVPRDPEALLPK 339
Cdd:COG5821   141 TVYANLdSKIKVKVGQKVKKGQVIGKVGSTALFESSEgphLHFEVLKNGKPVDPMKYLKK 200
nlpD PRK10871
murein hydrolase activator NlpD;
206-340 2.57e-20

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 89.89  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 206 WPAPGKVRRGFvarargaSSSEARSRrgapasphdGIDIAGAKGDPVRAAAPGLVWYAGKEPNLYGNVVIIDHGRGWFSA 285
Cdd:PRK10871  202 WPTDGKVIENF-------SASEGGNK---------GIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSA 265

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1893763502 286 YAKLSKVTVKKGELVRGGERVGLIGNTGsTSTTELHFEIRRNTVPRDPEALLPKR 340
Cdd:PRK10871  266 YAHNDTMLVREQQEVKAGQKIATMGSTG-TSSTRLHFEIRYKGKSVNPLRYLPQR 319
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 239-327 2.01e-14

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 71.18  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 239 HDGIDIAGAKGDPVRAAAPGLVWYAGKEPNlYGNVVIIDHGRGWFSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTT 318
Cdd:COG5833   120 GKGVDIETPGGANVKAVKEGYVIFAGKDEE-TGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPATEGEEGT 198


                  ....*....
gi 1893763502 319 eLHFEIRRN 327
Cdd:COG5833   199 -FYFAIKKG 206
PRK11649 PRK11649
putative peptidase; Provisional
 225-339 2.14e-14

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 73.55  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 225 SSEARSRRGAPA----SPHDGIDIAGAKGDPVRAAAPGLVWYAgKEPNLYGNVVIIDHGRGWFSAYAKLSKVTVKKGELV 300
Cdd:PRK11649  295 SSNFNPRRLNPVtgrvAPHRGVDFAMPVGTPVLAVGDGEVVVA-KRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKV 373

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1893763502 301 RGGERVGLIGNTGSTSTTELHFEIRRNTVPRDP-EALLPK 339
Cdd:PRK11649  374 KRGDRIALSGNTGRSTGPHLHYEVWINQQAVNPlTAKLPR 413
PRK11637 PRK11637
AmiB activator; Provisional
 206-326 3.84e-12

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 66.64  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502 206 WPAPGKVRRGFVARARGasssEARSRrgapasphdGIDIAGAKGDPVRAAAPGLV----WYAGkepnlYGNVVIIDHGRG 281
Cdd:PRK11637  309 WPVRGPTLHRFGEQLQG----ELRWK---------GMVIGASEGTEVKAIADGRVlladWLQG-----YGLVVVVEHGKG 370

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1893763502 282 WFSAYAKLSKVTVKKGELVRGGERVGLIGNTGSTSTTELHFEIRR 326
Cdd:PRK11637  371 DMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSLYFEIRR 415
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
41-150 3.81e-09

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 55.10  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893763502  41 PRGTEPAAESDPRTETRHVVRAGETLGGIANRAEVPriliieanalpppyavregqvlVIPRRRSHRVKEGETGFAIAMD 120
Cdd:COG1388    69 KAALAAAPEAAAAAAARYTVKSGDTLSGIARRYGAA----------------------AAPSPVTYTVKKGDTLWSIARR 126

                          90       100       110
                  ....*....|....*....|....*....|
gi 1893763502 121 YGVPWSAIAVANGIDPKgRVRAGQALVIPT 150
Cdd:COG1388   127 YGVSVEELKRWNGLSSD-TIRPGQKLKIPA 155
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 106-149 1.16e-08

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: 50.47  E-value: 1.16e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1893763502 106 HRVKEGETGFAIAMDYGVPWSAIAVANGIDPKgRVRAGQALVIP 149
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSP-NLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 104-148 2.36e-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: 2.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1893763502 104 RSHRVKEGETGFAIAMDYGVPWSAIAVANGIDPKGRVRAGQALVI 148
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 56-100 5.31e-07

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: 45.55  E-value: 5.31e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1893763502  56 TRHVVRAGETLGGIANRAEVPRILIIEANALPPPYAVREGQVLVI 100
Cdd:cd00118     1 KTYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 58-101 1.33e-06

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: 44.31  E-value: 1.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1893763502  58 HVVRAGETLGGIANRAEVPRILIIEANALPPPYaVREGQVLVIP 101
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSPN-LYVGQKLKIP 43
LysM smart00257
Lysin motif;
106-148 3.48e-06

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 43.20  E-value: 3.48e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1893763502  106 HRVKEGETGFAIAMDYGVPWSAIAVANGIDPKGRVRAGQALVI 148
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
49-103 2.32e-05

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 43.93  E-value: 2.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1893763502  49 ESDPRTETRHVVRAGETLGGIANRAEVPRILIIEANALpPPYAVREGQVLVIPRR 103
Cdd:COG1388   103 AAAAPSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGL-SSDTIRPGQKLKIPAS 156
LysM smart00257
Lysin motif;
58-100 2.66e-05

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 40.89  E-value: 2.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1893763502   58 HVVRAGETLGGIANRAEVPRILIIEANALPPPYAVREGQVLVI 100
Cdd:smart00257   2 YTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 38-102 2.57e-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: 41.14  E-value: 2.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1893763502  38 TASPRGTEPAAESDPRTETRHVVRAGETLGGIANR-----AEVPRILiiEAN--ALPPPYAVREGQVLVIPR 102
Cdd:COG1652    92 TVAEEAAAPSAELAPDAPKTYTVKPGDTLWGIAKRfygdpARWPEIA--EANrdQIKNPDLIYPGQVLRIPA 161
 
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.
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