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Conserved domains on  [gi|1403617589|emb|SQI51847|]
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nlpD [Acinetobacter baumannii]

Protein Classification

M23 peptidase family protein( domain architecture ID 1000974)

M23 peptidase family protein similar to murein hydrolase activator NlpD and to Haemophilus somni LppB lipoprotein outer membrane antigen, a putative virulence determinant; NlpD/LppB contains LysM and M23 peptidase domains

Gene Ontology:  GO:0004222|GO:0009279
MEROPS:  M23
PubMed:  19759820|8478068

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nlpD super family cl35964
murein hydrolase activator NlpD;
53-275 7.25e-45

murein hydrolase activator NlpD;


The actual alignment was detected with superfamily member PRK10871:

Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 153.84  E-value: 7.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589  53 NYYTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPYRIYVNQSLRLKKSS----SPRTVSTQ-------VMAQPEPIKRQT 121
Cdd:PRK10871   61 STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASgtpiTGGNAITQadaaeqgVVIKPAQNSTVA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 122 IA------------------------LPTTTAPTTTTPPPATVAPSTNTTVGASIPSSSLRWvkPNNGPVIQGFNLAN-N 176
Cdd:PRK10871  141 VAsqptitysessgeqsankmlpnnkPAATTVTAPVTAPTASTTEPTASSTSTSTPISTWRW--PTDGKVIENFSASEgG 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 177 VKGIRYGGNQGDPIYAAADGQVVYAADGLKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGASRVM 256
Cdd:PRK10871  219 NKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTR 298

                         250
                  ....*....|....*....
gi 1403617589 257 LEFQIRLDGKPINPANLLP 275
Cdd:PRK10871  299 LHFEIRYKGKSVNPLRYLP 317
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
53-275 7.25e-45

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 153.84  E-value: 7.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589  53 NYYTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPYRIYVNQSLRLKKSS----SPRTVSTQ-------VMAQPEPIKRQT 121
Cdd:PRK10871   61 STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASgtpiTGGNAITQadaaeqgVVIKPAQNSTVA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 122 IA------------------------LPTTTAPTTTTPPPATVAPSTNTTVGASIPSSSLRWvkPNNGPVIQGFNLAN-N 176
Cdd:PRK10871  141 VAsqptitysessgeqsankmlpnnkPAATTVTAPVTAPTASTTEPTASSTSTSTPISTWRW--PTDGKVIENFSASEgG 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 177 VKGIRYGGNQGDPIYAAADGQVVYAADGLKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGASRVM 256
Cdd:PRK10871  219 NKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTR 298

                         250
                  ....*....|....*....
gi 1403617589 257 LEFQIRLDGKPINPANLLP 275
Cdd:PRK10871  299 LHFEIRYKGKSVNPLRYLP 317
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 145-275 6.55e-40

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: 142.21  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 145 NTTVGASIPSSSLRWVKPNNGPVIQGFNLANNV----KGIRYGGNQGDPIYAAADGQVVYAaDGLKEYGNLVLIKHIDGY 220
Cdd:COG4942   241 ERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGggrnKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHGGGY 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1403617589 221 ISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVMLEFQIRLDGKPINPANLLP 275
Cdd:COG4942   320 LTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQgGPTLYFELRKNGKPVDPLPWLA 375
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 178-270 3.61e-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: 119.19  E-value: 3.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 178 KGIRYGGNQGDPIYAAADGQVVYAADgLKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVM 256
Cdd:pfam01551   4 KGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRStGPH 82

                          90
                  ....*....|....
gi 1403617589 257 LEFQIRLDGKPINP 270
Cdd:pfam01551  83 LHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 178-261 2.67e-26

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: 98.43  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 178 KGIRYGGNQGDPIYAAADGQVVYAADGlKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVM 256
Cdd:cd12797     2 NGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRStGPH 80


                  ....*
gi 1403617589 257 LEFQI 261
Cdd:cd12797    81 LHFEI 85
LysM smart00257
Lysin motif;
54-97 3.65e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 3.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1403617589   54 YYTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPYRIYVNQSLRL 97
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
nlpD PRK10871
murein hydrolase activator NlpD;
53-275 7.25e-45

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 153.84  E-value: 7.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589  53 NYYTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPYRIYVNQSLRLKKSS----SPRTVSTQ-------VMAQPEPIKRQT 121
Cdd:PRK10871   61 STYTVKKGDTLFYIAWITGNDFRDLAQRNNIQAPYSLNVGQTLQVGNASgtpiTGGNAITQadaaeqgVVIKPAQNSTVA 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 122 IA------------------------LPTTTAPTTTTPPPATVAPSTNTTVGASIPSSSLRWvkPNNGPVIQGFNLAN-N 176
Cdd:PRK10871  141 VAsqptitysessgeqsankmlpnnkPAATTVTAPVTAPTASTTEPTASSTSTSTPISTWRW--PTDGKVIENFSASEgG 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 177 VKGIRYGGNQGDPIYAAADGQVVYAADGLKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGASRVM 256
Cdd:PRK10871  219 NKGIDIAGSKGQAIIATADGRVVYAGNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSSTR 298

                         250
                  ....*....|....*....
gi 1403617589 257 LEFQIRLDGKPINPANLLP 275
Cdd:PRK10871  299 LHFEIRYKGKSVNPLRYLP 317
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 145-275 6.55e-40

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: 142.21  E-value: 6.55e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 145 NTTVGASIPSSSLRWVKPNNGPVIQGFNLANNV----KGIRYGGNQGDPIYAAADGQVVYAaDGLKEYGNLVLIKHIDGY 220
Cdd:COG4942   241 ERTPAAGFAALKGKLPWPVSGRVVRRFGERDGGggrnKGIDIAAPPGAPVRAVADGTVVYA-GWLRGYGNLVIIDHGGGY 319

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1403617589 221 ISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVMLEFQIRLDGKPINPANLLP 275
Cdd:COG4942   320 LTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQgGPTLYFELRKNGKPVDPLPWLA 375
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 108-275 8.50e-40

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: 137.03  E-value: 8.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 108 TQVMAQPEPIKRQTIALPTTTAPTTTTPPPATVAPSTNTTVGASIPSSSLRWvkPNNGPVIQGFNLANNV--------KG 179
Cdd:COG0739    22 GAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAW--PVKGRITSGFGYRRHPvtgrrrfhKG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 180 IRYGGNQGDPIYAAADGQVVYAADGlKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVMLE 258
Cdd:COG0739   100 IDIAAPTGTPVYAAADGTVVFAGWN-GGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRStGPHLH 178

                         170
                  ....*....|....*..
gi 1403617589 259 FQIRLDGKPINPANLLP 275
Cdd:COG0739   179 FEVRVNGKPVDPLPFLP 195
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 178-270 3.61e-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: 119.19  E-value: 3.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 178 KGIRYGGNQGDPIYAAADGQVVYAADgLKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVM 256
Cdd:pfam01551   4 KGIDIAAPTGTPVYAAADGVVVFAGW-LGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRStGPH 82

                          90
                  ....*....|....
gi 1403617589 257 LEFQIRLDGKPINP 270
Cdd:pfam01551  83 LHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 178-261 2.67e-26

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: 98.43  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 178 KGIRYGGNQGDPIYAAADGQVVYAADGlKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGAS-RVM 256
Cdd:cd12797     2 NGIDIAAPEGTPVYAAADGTVVFAGWD-GGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRStGPH 80


                  ....*
gi 1403617589 257 LEFQI 261
Cdd:cd12797    81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 143-275 9.39e-26

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: 100.49  E-value: 9.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 143 STNTTVGASIPSSSLRWVKPNNGPVIQGFNLANNV----------KGIRYGGNQGDPIYAAADGQVVYAADGlKEYGNLV 212
Cdd:COG5821    53 SNEKSKSKVTASTSNKFLKPVSGKITREFGEDLVYsktlnewrthTGIDIAAKEGTPVKAAADGVVVEVGKD-PKYGITV 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403617589 213 LIKHIDGYISAYAH-NSKMMVKSGDNVTAGQKIAEMGSSGASRVM----LEFQIRLDGKPINPANLLP 275
Cdd:COG5821   132 VIDHGNGIKTVYANlDSKIKVKVGQKVKKGQVIGKVGSTALFESSegphLHFEVLKNGKPVDPMKYLK 199
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 159-275 2.26e-18

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 81.19  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 159 WVKPNNGPVIQGFnlANNVKGIRYGGNQGDPIYAAADGQVVYAADGlKEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNV 238
Cdd:COG5833   104 FALPVSGKVVESF--QENGKGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVIIQHADGSESWYGNLSSIDVKLYDFV 180

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1403617589 239 TAGQKIAEMGSSGASRVMLEFQIRLDGKPINPANLLP 275
Cdd:COG5833   181 EAGQKIGTVPATEGEEGTFYFAIKKGGKFIDPIQVIS 217
PRK11637 PRK11637
AmiB activator; Provisional
 147-270 4.46e-15

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 74.34  E-value: 4.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 147 TVGASIPSSSLRWvkPNNGPVIQGFN--LANNV--KGIRYGGNQGDPIYAAADGQVVYAaDGLKEYGNLVLIKHIDGYIS 222
Cdd:PRK11637  297 TGGLGRPRGQAFW--PVRGPTLHRFGeqLQGELrwKGMVIGASEGTEVKAIADGRVLLA-DWLQGYGLVVVVEHGKGDMS 373

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1403617589 223 AYAHNSKMMVKSGDNVTAGQKIAEMGSSGA-SRVMLEFQIRLDGKPINP 270
Cdd:PRK11637  374 LYGYNQSALVSVGAQVRAGQPIALVGSSGGqGRPSLYFEIRRQGQAVNP 422
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 54-97 1.41e-12

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: 60.96  E-value: 1.41e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1403617589  54 YYTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPYRIYVNQSLRL 97
Cdd:cd00118     2 TYTVKPGDTLWSIAKKYGVTVEELAAANPLINPDCIYPGQKLKI 45
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 55-98 6.24e-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: 56.25  E-value: 6.24e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1403617589  55 YTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPyRIYVNQSLRLK 98
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQLAELNGLSSP-NLYVGQKLKIP 43
LysM smart00257
Lysin motif;
54-97 3.65e-10

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 53.99  E-value: 3.65e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1403617589   54 YYTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPYRIYVNQSLRL 97
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISVSDLLELNNILDPDNLQVGQKLKI 44
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
49-100 6.72e-10

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


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 56.64  E-value: 6.72e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1403617589  49 AMAPNYYTVRSGDTLSGIAMRYGLDYLSIAEMNGIApPYRIYVNQSLRLKKS 100
Cdd:COG1388   106 APSPVTYTVKKGDTLWSIARRYGVSVEELKRWNGLS-SDTIRPGQKLKIPAS 156
XkdP COG1652
Cytoplasmic potassium-binding protein Kbp/XkdP/YgaU, contains LysM domain [Inorganic ion ...
 51-97 7.25e-10

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: 56.55  E-value: 7.25e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1403617589  51 APNYYTVRSGDTLSGIAMRY---GLDYLSIAEMN--GIAPPYRIYVNQSLRL 97
Cdd:COG1652   108 APKTYTVKPGDTLWGIAKRFygdPARWPEIAEANrdQIKNPDLIYPGQVLRI 159
PRK11649 PRK11649
putative peptidase; Provisional
 178-270 1.56e-09

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 58.14  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589 178 KGIRYGGNQGDPIYAAADGQVVYAA-DGlkEYGNLVLIKHIDGYISAYAHNSKMMVKSGDNVTAGQKIAEMGSSGASR-V 255
Cdd:PRK11649  314 RGVDFAMPVGTPVLAVGDGEVVVAKrSG--AAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTgP 391

                          90
                  ....*....|....*
gi 1403617589 256 MLEFQIRLDGKPINP 270
Cdd:PRK11649  392 HLHYEVWINQQAVNP 406
PRK11198 PRK11198
LysM domain/BON superfamily protein; Provisional
 49-99 4.81e-05

LysM domain/BON superfamily protein; Provisional


Pssm-ID: 236880 [Multi-domain]  Cd Length: 147  Bit Score: 42.59  E-value: 4.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1403617589  49 AMAPNYYTVRSGDTLSGIAMRY---GLDYLSIAEMNG--IAPPYRIYVNQSLRLKK 99
Cdd:PRK11198   92 APESQFYTVKSGDTLSAIAKKVygnANKYNKIFEANKpmLKSPDKIYPGQVLRIPE 147
mltD PRK10783
membrane-bound lytic murein transglycosylase D; Provisional
 55-108 1.92e-04

membrane-bound lytic murein transglycosylase D; Provisional


Pssm-ID: 182727 [Multi-domain]  Cd Length: 456  Bit Score: 42.41  E-value: 1.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1403617589  55 YTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPyRIYVNQSLRLKKSSSPRTVST 108
Cdd:PRK10783  346 YKVRSGDTLSGIASRLNVSTKDLQQWNNLRGS-KLKVGQTLTIGAGSSAQRLAN 398
PRK06148 PRK06148
hypothetical protein; Provisional
 187-264 2.55e-04

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 42.32  E-value: 2.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403617589  187 GDPIYAAADGQVVYA---ADGLkEYGNLVLIKH----IDGYISAY---AHNSKMMVKSGDNVTAGQKIAEMGS---SGAS 253
Cdd:PRK06148   451 GTPVYAPLAGTVRSVeieAVPL-GYGGLVALEHetpgGDPFYTLYghlAHEAVSRLKPGDRLAAGELFGAMGDaheNGGW 529

                           90
                   ....*....|.
gi 1403617589  254 RVMLEFQIRLD 264
Cdd:PRK06148   530 APHLHFQLSTD 540
PRK13914 PRK13914
invasion associated endopeptidase;
55-121 1.38e-03

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 39.78  E-value: 1.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403617589  55 YTVRSGDTLSGIAMRYGLDYLSIAEMNGIAPPyRIYVNQSLRLKKSSSPRTVSTQVMAQPEPIKRQT 121
Cdd:PRK13914  202 HAVKSGDTIWALSVKYGVSVQDIMSWNNLSSS-SIYVGQKLAIKQTANTATPKAEVKTEAPAAEKQA 267
 
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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