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Conserved domains on  [gi|446641959|ref|WP_000719305|]
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MULTISPECIES: LPXTG cell wall anchor domain-containing protein [Bacillus]

Protein Classification

LPXTG cell wall anchor domain-containing protein( domain architecture ID 13410896)

LPXTG cell wall anchor domain-containing protein similar to Streptococcus mutans collagen-binding adhesin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
iso_D2_wall_anc super family cl41511
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
20-549 4.37e-28

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


The actual alignment was detected with superfamily member NF033902:

Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 117.93  E-value: 4.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  20 SVLVKADSPSKGTLTIHKYEQEKDGAQGleGDGSANQEVPKDVKPLKGVTFEVKRV-----------ASFEKISNDGKIV 88
Cdd:NF033902  42 AGNIDLDKTGTSSITIHKYLGPPATGTG--GGTKGTGDSAAGGKPLKGVTFTITKVtkidlttnagwAKIAKLTTAAAGT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  89 KEDVKPVMGATPNQV----VTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVDIPLTNKEGKVL--NYDVHMYPK 162
Cdd:NF033902 120 AAAFATTLGDTTKTTtttgTTDADGTAKFSNLPLGLYLVEETDAPYSVVVKAAPFLVTVPLTNPTGNATkwNYDVHVYPK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 163 NEIKRGAVDLIKTgvnekalagavfslfkkdgtevkkelVTDANGhirvqgleygeyyfqetkapkgyvidptkreffvk 242
Cdd:NF033902 200 NQKLSDKVTKTKD--------------------------VTDAVG----------------------------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 243 nsgtinedgtitsgtvvkievknneePTIDKKINgklealpinpltnynYDIKTLIPEDIKE----YKKYVVTDTLDNRL 318
Cdd:NF033902 219 --------------------------NGVGDTIT---------------YTITAPVPKIDANtlddFKGFTVTDTLDTRL 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 319 VIQGKPIVKIDGAEVNANVVEVAIE-----------GQKVTATVKDF--TKLDGKK--EFHLQIKSQVKEGVPSGS--EI 381
Cdd:NF033902 258 DEVAGVVKSVKVGGTGLTATLTVTTdytvttdgltaDQKVTVTFTEAglAKLAAAKnvKVTVTFKTKVTKTAKGGTngEI 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 382 LNTAKIHFTNKN-------DVIGEKESKPVVVipTTGIIELTKIDS-ANKNKLKGAEFVL---KDNNGKIVVVA---GKE 447
Cdd:NF033902 338 TNKAGLIPNNPGpntpeptTPGTPDPTPTVKT--YFGKLKIKKVDAdDTSKKLKGAEFKVyacEADAAAACVNAigiNGK 415
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 448 VTGVSDENGVIKWS--------------NIPYGDYQIFETKAPtytkedgtkASYQLLKDPIDVKISENNQT------VK 507
Cdd:NF033902 416 TTFTTGADGTVSIDglhvtdledgasvkAAAGKDYCLVETKAP---------AGYVLPPKPVEVTVVKVTVTaattadVK 486
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 446641959 508 LTIENNKSGW-----ILPVTGGIGTTLFTVIGLTLMLTAAFVFFRKK 549
Cdd:NF033902 487 NTVVNNKKTVpnwffNLPLTGGAGVIILAAAGAALLGAGAFVALRNR 533
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
177-245 7.67e-17

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


:

Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 74.93  E-value: 7.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446641959  177 VNEKALAGAVFSLFKKDGT---EVKKELVTDANGHIRVQGLEYGEYYFQETKAPKGYVIDPTKREFFVKNSG 245
Cdd:pfam17802   1 DTGKPLAGAEFTLYDADGTvdgKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTPIEFTVTEDG 72
 
Name Accession Description Interval E-value
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
20-549 4.37e-28

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 117.93  E-value: 4.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  20 SVLVKADSPSKGTLTIHKYEQEKDGAQGleGDGSANQEVPKDVKPLKGVTFEVKRV-----------ASFEKISNDGKIV 88
Cdd:NF033902  42 AGNIDLDKTGTSSITIHKYLGPPATGTG--GGTKGTGDSAAGGKPLKGVTFTITKVtkidlttnagwAKIAKLTTAAAGT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  89 KEDVKPVMGATPNQV----VTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVDIPLTNKEGKVL--NYDVHMYPK 162
Cdd:NF033902 120 AAAFATTLGDTTKTTtttgTTDADGTAKFSNLPLGLYLVEETDAPYSVVVKAAPFLVTVPLTNPTGNATkwNYDVHVYPK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 163 NEIKRGAVDLIKTgvnekalagavfslfkkdgtevkkelVTDANGhirvqgleygeyyfqetkapkgyvidptkreffvk 242
Cdd:NF033902 200 NQKLSDKVTKTKD--------------------------VTDAVG----------------------------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 243 nsgtinedgtitsgtvvkievknneePTIDKKINgklealpinpltnynYDIKTLIPEDIKE----YKKYVVTDTLDNRL 318
Cdd:NF033902 219 --------------------------NGVGDTIT---------------YTITAPVPKIDANtlddFKGFTVTDTLDTRL 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 319 VIQGKPIVKIDGAEVNANVVEVAIE-----------GQKVTATVKDF--TKLDGKK--EFHLQIKSQVKEGVPSGS--EI 381
Cdd:NF033902 258 DEVAGVVKSVKVGGTGLTATLTVTTdytvttdgltaDQKVTVTFTEAglAKLAAAKnvKVTVTFKTKVTKTAKGGTngEI 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 382 LNTAKIHFTNKN-------DVIGEKESKPVVVipTTGIIELTKIDS-ANKNKLKGAEFVL---KDNNGKIVVVA---GKE 447
Cdd:NF033902 338 TNKAGLIPNNPGpntpeptTPGTPDPTPTVKT--YFGKLKIKKVDAdDTSKKLKGAEFKVyacEADAAAACVNAigiNGK 415
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 448 VTGVSDENGVIKWS--------------NIPYGDYQIFETKAPtytkedgtkASYQLLKDPIDVKISENNQT------VK 507
Cdd:NF033902 416 TTFTTGADGTVSIDglhvtdledgasvkAAAGKDYCLVETKAP---------AGYVLPPKPVEVTVVKVTVTaattadVK 486
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 446641959 508 LTIENNKSGW-----ILPVTGGIGTTLFTVIGLTLMLTAAFVFFRKK 549
Cdd:NF033902 487 NTVVNNKKTVpnwffNLPLTGGAGVIILAAAGAALLGAGAFVALRNR 533
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
267-389 9.62e-21

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 88.09  E-value: 9.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  267 EEPTIDKKINGKLEALpINPLTNYNYDIKTLIPEDIKEYKKYVVTDTLDNRLVIQGKPIVKIDGAEVNANVVEVAIEGQK 346
Cdd:TIGR04226   1 EEPTITKKVNDKDDAD-VNIGDEVTYTITTTVPADIADYKSFVITDTLDDGLTYKGSVKVTVDGKTLTVDTDYTVTDGQT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446641959  347 VTATVKD-FTKLDGKKEFHLQIKSQVKEGVPSGSEILNTAKIHF 389
Cdd:TIGR04226  80 VTVTFTDaGLKKLAGKKITVTYTAKVKEGAVLGKGIPNTATLTY 123
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
103-518 1.96e-20

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 95.42  E-value: 1.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 103 VVTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVDIPltnkEGKVLNYDVhMYPKNEIKRGAVDLIKTGVN--EK 180
Cdd:COG4932  298 TVTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTIT----AGQTTTVTV-TNGNNEVKTGSVTLTKVDADdgEA 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 181 ALAGAVFSLFKKDGTEVKkELVTDANGHIRVQGLEYGEYYFQETKAPKGYVIDPTKREFfvknsgtinedgTITSGTVVK 260
Cdd:COG4932  373 PLAGAEFTLTDADGTVVA-TITTDADGTASFKGLAPGTYTLTETKAPEGYTLDSTPITV------------TVTDGGTGA 439
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 261 IEVKNNEEPTIDKKINGKLEALPINPLTNYNYDIKTLIPEDIKEYKKYVVTDTLDNRLVIQGKPIVKIDGAEVNANVVEV 340
Cdd:COG4932  440 IDTITNERKKGSVQVTKVDAPLAGATFTLTDADGTVVTLTTDADLAGATFEADGKVVTTTDASGKYTFKNLPPGTYTDAG 519
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 341 AIEGQKVTATVKDFTKLDGKKEFHLQIKSQVKEGVPSGSEILNTAKIHFTNKNDVIGEKESKPVVVIPTTGIIELTKids 420
Cdd:COG4932  520 GSATVITDDTDGTVGDEATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLD--- 596
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 421 anknklKGAEFVLKDNNGKIVVVAGKEVTGVSDENGVIKWSNIPYGDYQIFETKAPTYTKEDGTKASYQLLKDPIDVKIS 500
Cdd:COG4932  597 ------TNATEKTETVTVTAQLIGVKTTKLTDTTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTT 670
                        410
                 ....*....|....*...
gi 446641959 501 ENNQTVKLTIENNKSGWI 518
Cdd:COG4932  671 DVDNKDAFTGGTEPGGTI 688
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
177-245 7.67e-17

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 74.93  E-value: 7.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446641959  177 VNEKALAGAVFSLFKKDGT---EVKKELVTDANGHIRVQGLEYGEYYFQETKAPKGYVIDPTKREFFVKNSG 245
Cdd:pfam17802   1 DTGKPLAGAEFTLYDADGTvdgKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTPIEFTVTEDG 72
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
422-503 4.57e-12

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 61.45  E-value: 4.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  422 NKNKLKGAEFVLKDNNGKIVVVAGKEVTgvSDENGVIKWSNIPYGDYQIFETKAPtytkedgtkASYQLLKDPIDVKISE 501
Cdd:pfam17802   2 TGKPLAGAEFTLYDADGTVDGKVVGTLT--TDEDGKATFDGLPPGTYTLKETKAP---------DGYVLDDTPIEFTVTE 70

                  ..
gi 446641959  502 NN 503
Cdd:pfam17802  71 DG 72
 
Name Accession Description Interval E-value
iso_D2_wall_anc NF033902
SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits ...
20-549 4.37e-28

SpaH/EbpB family LPXTG-anchored major pilin; Members of this family are pilin major subunits whose structure includes an LPXTG motif-containing signal (see TIGR01167) near the C-terminus, for processing by sortases. Most contain a recognizable D2-type fimbrial isopeptide formation domain (see TIGR04226), in which Lys-to-Asn isopeptide bond formation provides additional structural integrity to support adhesion despite shear. For proper members of this subfamily, lengths fall typically in the range of 460 to 640 amino acids in length. Many members of this family contribute to the virulence of certain Gram-positive pathogens, including SpaA, SpaD, and SpaH from Corynebacterium diphtheriae, and EbpB and EbpC from Enterococcus faecalis.


Pssm-ID: 468234 [Multi-domain]  Cd Length: 533  Bit Score: 117.93  E-value: 4.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  20 SVLVKADSPSKGTLTIHKYEQEKDGAQGleGDGSANQEVPKDVKPLKGVTFEVKRV-----------ASFEKISNDGKIV 88
Cdd:NF033902  42 AGNIDLDKTGTSSITIHKYLGPPATGTG--GGTKGTGDSAAGGKPLKGVTFTITKVtkidlttnagwAKIAKLTTAAAGT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  89 KEDVKPVMGATPNQV----VTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVDIPLTNKEGKVL--NYDVHMYPK 162
Cdd:NF033902 120 AAAFATTLGDTTKTTtttgTTDADGTAKFSNLPLGLYLVEETDAPYSVVVKAAPFLVTVPLTNPTGNATkwNYDVHVYPK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 163 NEIKRGAVDLIKTgvnekalagavfslfkkdgtevkkelVTDANGhirvqgleygeyyfqetkapkgyvidptkreffvk 242
Cdd:NF033902 200 NQKLSDKVTKTKD--------------------------VTDAVG----------------------------------- 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 243 nsgtinedgtitsgtvvkievknneePTIDKKINgklealpinpltnynYDIKTLIPEDIKE----YKKYVVTDTLDNRL 318
Cdd:NF033902 219 --------------------------NGVGDTIT---------------YTITAPVPKIDANtlddFKGFTVTDTLDTRL 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 319 VIQGKPIVKIDGAEVNANVVEVAIE-----------GQKVTATVKDF--TKLDGKK--EFHLQIKSQVKEGVPSGS--EI 381
Cdd:NF033902 258 DEVAGVVKSVKVGGTGLTATLTVTTdytvttdgltaDQKVTVTFTEAglAKLAAAKnvKVTVTFKTKVTKTAKGGTngEI 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 382 LNTAKIHFTNKN-------DVIGEKESKPVVVipTTGIIELTKIDS-ANKNKLKGAEFVL---KDNNGKIVVVA---GKE 447
Cdd:NF033902 338 TNKAGLIPNNPGpntpeptTPGTPDPTPTVKT--YFGKLKIKKVDAdDTSKKLKGAEFKVyacEADAAAACVNAigiNGK 415
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 448 VTGVSDENGVIKWS--------------NIPYGDYQIFETKAPtytkedgtkASYQLLKDPIDVKISENNQT------VK 507
Cdd:NF033902 416 TTFTTGADGTVSIDglhvtdledgasvkAAAGKDYCLVETKAP---------AGYVLPPKPVEVTVVKVTVTaattadVK 486
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*..
gi 446641959 508 LTIENNKSGW-----ILPVTGGIGTTLFTVIGLTLMLTAAFVFFRKK 549
Cdd:NF033902 487 NTVVNNKKTVpnwffNLPLTGGAGVIILAAAGAALLGAGAFVALRNR 533
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
267-389 9.62e-21

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 88.09  E-value: 9.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  267 EEPTIDKKINGKLEALpINPLTNYNYDIKTLIPEDIKEYKKYVVTDTLDNRLVIQGKPIVKIDGAEVNANVVEVAIEGQK 346
Cdd:TIGR04226   1 EEPTITKKVNDKDDAD-VNIGDEVTYTITTTVPADIADYKSFVITDTLDDGLTYKGSVKVTVDGKTLTVDTDYTVTDGQT 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 446641959  347 VTATVKD-FTKLDGKKEFHLQIKSQVKEGVPSGSEILNTAKIHF 389
Cdd:TIGR04226  80 VTVTFTDaGLKKLAGKKITVTYTAKVKEGAVLGKGIPNTATLTY 123
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
103-518 1.96e-20

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 95.42  E-value: 1.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 103 VVTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVDIPltnkEGKVLNYDVhMYPKNEIKRGAVDLIKTGVN--EK 180
Cdd:COG4932  298 TVTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKVTIT----AGQTTTVTV-TNGNNEVKTGSVTLTKVDADdgEA 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 181 ALAGAVFSLFKKDGTEVKkELVTDANGHIRVQGLEYGEYYFQETKAPKGYVIDPTKREFfvknsgtinedgTITSGTVVK 260
Cdd:COG4932  373 PLAGAEFTLTDADGTVVA-TITTDADGTASFKGLAPGTYTLTETKAPEGYTLDSTPITV------------TVTDGGTGA 439
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 261 IEVKNNEEPTIDKKINGKLEALPINPLTNYNYDIKTLIPEDIKEYKKYVVTDTLDNRLVIQGKPIVKIDGAEVNANVVEV 340
Cdd:COG4932  440 IDTITNERKKGSVQVTKVDAPLAGATFTLTDADGTVVTLTTDADLAGATFEADGKVVTTTDASGKYTFKNLPPGTYTDAG 519
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 341 AIEGQKVTATVKDFTKLDGKKEFHLQIKSQVKEGVPSGSEILNTAKIHFTNKNDVIGEKESKPVVVIPTTGIIELTKids 420
Cdd:COG4932  520 GSATVITDDTDGTVGDEATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLD--- 596
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 421 anknklKGAEFVLKDNNGKIVVVAGKEVTGVSDENGVIKWSNIPYGDYQIFETKAPTYTKEDGTKASYQLLKDPIDVKIS 500
Cdd:COG4932  597 ------TNATEKTETVTVTAQLIGVKTTKLTDTTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTT 670
                        410
                 ....*....|....*...
gi 446641959 501 ENNQTVKLTIENNKSGWI 518
Cdd:COG4932  671 DVDNKDAFTGGTEPGGTI 688
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
17-522 3.36e-20

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 94.65  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  17 TWSSVLVKADSPSKGTLTIHKYEQEKDGAQGLEGDGSANQEVPKDVKPLKGVTFEVKRVASFEKISNDGKIVKEDVKPVM 96
Cdd:COG4932   18 GAGSGSLVAVTTGAVLGLALGSTGGTAGSAAAINSAPATGTATGTSAGATAVIVIAAGLTATPTETASGLGGDATVTTTA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  97 GATPNQVVTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVDIPLTNKEGKVLNYDVHMYPKNEIKrgaVDLIKTG 176
Cdd:COG4932   98 NVAKVTNGAAANLTVNADGTASNAGTLAKGAETATGNLDGDAGDVTVTAAATDGVNDVDGNGASVTDSVT---LKKVDDG 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 177 VNEKALAGAVFSLFKKDGTEVKkELVTDANGHIRVQGLEYGEYYFQETKAPKGYVIDPtkreffvKNSGTINEDGTITSG 256
Cdd:COG4932  175 DTGKPLPGATFTLYDSDGTLVK-TVTTDADGKYTFTDLPPGTYTLTETKAPEGYVLDT-------KDPTGATITVTVNAG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 257 TVVKIEVKNNEEPTIDKKINGKLEALPINPLTNynydiktlipedikeyKKYVVTDTLDNRLViqgkpivkidgaevnan 336
Cdd:COG4932  247 GTVTVTLKNTPKYTKGSVTVTKTDADTGEPLAG----------------ATFTLTDADGNTVV----------------- 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 337 vvevaieGQKVTATVKDftkldGKKEFHLQI--KSQVKEGVPSGSEILNTAKIHFTNKNDVIGEKESKPVVVIPTTGIIE 414
Cdd:COG4932  294 -------TTTVTVTDAD-----GSYTFTDLPpgTYTVTETKAPAGYDLDGEAVKVTITAGQTTTVTVTNGNNEVKTGSVT 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 415 LTKIDSANKNK-LKGAEFVLKDNNGKIVVvagkevTGVSDENGVIKWSNIPYGDYQIFETKAPTytkedgtkaSYQLLKD 493
Cdd:COG4932  362 LTKVDADDGEApLAGAEFTLTDADGTVVA------TITTDADGTASFKGLAPGTYTLTETKAPE---------GYTLDST 426
                        490       500
                 ....*....|....*....|....*....
gi 446641959 494 PIDVKISENNQTVKLTIENNKSGWILPVT 522
Cdd:COG4932  427 PITVTVTDGGTGAIDTITNERKKGSVQVT 455
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
177-245 7.67e-17

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 74.93  E-value: 7.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446641959  177 VNEKALAGAVFSLFKKDGT---EVKKELVTDANGHIRVQGLEYGEYYFQETKAPKGYVIDPTKREFFVKNSG 245
Cdd:pfam17802   1 DTGKPLAGAEFTLYDADGTvdgKVVGTLTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTPIEFTVTEDG 72
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
97-528 1.06e-14

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 77.32  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  97 GATPNQVVTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNP-NTYTVDIPLTNKEGKVlnYDVHMYPKNEIKRGAVDLIKT 175
Cdd:COG4932  192 GTLVKTVTTDADGKYTFTDLPPGTYTLTETKAPEGYVLDTkDPTGATITVTVNAGGT--VTVTLKNTPKYTKGSVTVTKT 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 176 -GVNEKALAGAVFSLFKKDGTEVKKELV--TDANGHIRVQGLEYGEYYFQETKAPKGYVIDPTKREFfvknsgtinedgT 252
Cdd:COG4932  270 dADTGEPLAGATFTLTDADGNTVVTTTVtvTDADGSYTFTDLPPGTYTVTETKAPAGYDLDGEAVKV------------T 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 253 ITSGTVVKIEVKNNEEPTIDKKINGklealpinpltnynydiktlipedikeykkyVVTDTLDNRLVIQGkpiVKIDGAE 332
Cdd:COG4932  338 ITAGQTTTVTVTNGNNEVKTGSVTL-------------------------------TKVDADDGEAPLAG---AEFTLTD 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 333 VNANVVEVAIEGQKVTATVKDFtkLDGKkefhlqikSQVKEGVPSGSEILNTAKIHFTNKNDviGEKESKPVVVIPTTGI 412
Cdd:COG4932  384 ADGTVVATITTDADGTASFKGL--APGT--------YTLTETKAPEGYTLDSTPITVTVTDG--GTGAIDTITNERKKGS 451
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959 413 IELTKIDsankNKLKGAEFVLKDNNGKIV------------VVAGKEVTGVSDENGVIKWSNIPYGDYQIFETKAPTYTK 480
Cdd:COG4932  452 VQVTKVD----APLAGATFTLTDADGTVVtlttdadlagatFEADGKVVTTTDASGKYTFKNLPPGTYTDAGGSATVITD 527
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 446641959 481 EDGTKASYQLLKDPIDVKISENNQTVKLTIENNKSGWILPVTGGIGTT 528
Cdd:COG4932  528 DTDGTVGDEATGTDPEVTVTGKSTTTTPDVALLTNLGTTEDALTSLAK 575
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
422-503 4.57e-12

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 61.45  E-value: 4.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  422 NKNKLKGAEFVLKDNNGKIVVVAGKEVTgvSDENGVIKWSNIPYGDYQIFETKAPtytkedgtkASYQLLKDPIDVKISE 501
Cdd:pfam17802   2 TGKPLAGAEFTLYDADGTVDGKVVGTLT--TDEDGKATFDGLPPGTYTLKETKAP---------DGYVLDDTPIEFTVTE 70

                  ..
gi 446641959  502 NN 503
Cdd:pfam17802  71 DG 72
GramPos_pilinD1 pfam16555
Gram-positive pilin subunit D1, N-terminal domain; GramPos_pilinD1 is the first subunit domain ...
28-164 6.36e-08

Gram-positive pilin subunit D1, N-terminal domain; GramPos_pilinD1 is the first subunit domain of Gram-positive pilins from Strep.pneumoniae. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three Ig-like, CnaB, domains along with a crucial N-terminal domain, D1. The three IG-like domains are stabilized by internal Lys-Asn isopeptide bonds, but this N-terminal domain makes few contact with the rest of the molecule due to the different orientation of its G beta-strand. Strand G of D1 also carries the YPKN motif that provides the essential Lys residue for the sortase-mediated intermolecular linkages along the pilus shaft. Gram-positive pili are formed from a single chain of covalently linked subunit proteins (pilins), usually comprising an adhesin at the distal tip, a major pilin that forms the polymer shaft and a minor pilin that mediates cell wall anchoring at the base.


Pssm-ID: 465172  Cd Length: 161  Bit Score: 52.42  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959   28 PSKGTLTIHKYEQ------EKDGAQGLEGDGSANQEvpKDVKPLKGVTFEVKRV-ASFEKISNDGKIVKEDVK------- 93
Cdd:pfam16555   1 TDTVTVTLHKRLFddgqlpEWKQNDGTEISGDADFG--DDGKPLNGVTFTVYDVtDEFYELRKTGLTTEEAIEklaklaa 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959   94 -----PVMGATPNQVVTDDNGQAVLKDLPL------GRYEVKEVAGPPHVNLNpnTYTVDI----PLTNKEGKVLNyDVH 158
Cdd:pfam16555  79 ddagaPALKKILTTQTTGEDGLATFTNLPLnsggrdGVYLFVETKSPSTTLTD--KKAVPFvlvlPVYNPDGNVLT-DIH 155

                  ....*.
gi 446641959  159 MYPKNE 164
Cdd:pfam16555 156 LYPKNT 161
SpaA pfam17802
Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety ...
63-147 6.88e-08

Prealbumin-like fold domain; This entry contains a prealbumin-like domain from a wide variety of bacterial surface proteins. This entry corresponds to domain 1 and domain 3 of SpaA from Corynebacterium diphtheriae. Some members of this family contain an isopeptide bond.


Pssm-ID: 465513 [Multi-domain]  Cd Length: 72  Bit Score: 49.51  E-value: 6.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959   63 KPLKGVTFEVKRVASfekiSNDGKIVKEdvkpvmgatpnqVVTDDNGQAVLKDLPLGRYEVKEVAGPPHVNLNPNTYTVD 142
Cdd:pfam17802   4 KPLAGAEFTLYDADG----TVDGKVVGT------------LTTDEDGKATFDGLPPGTYTLKETKAPDGYVLDDTPIEFT 67

                  ....*
gi 446641959  143 IPLTN 147
Cdd:pfam17802  68 VTEDG 72
LPXTG_anchor TIGR01167
LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region ...
518-549 3.30e-05

LPXTG-motif cell wall anchor domain; This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other]


Pssm-ID: 273478 [Multi-domain]  Cd Length: 34  Bit Score: 40.92  E-value: 3.30e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446641959  518 ILPVTGGIGTTLFTVIGLTLMLTAAFVFFRKK 549
Cdd:TIGR01167   1 KLPKTGESGNSLLLLLGLLLLGLGGLLLRKRK 32
Gram_pos_anchor pfam00746
LPXTG cell wall anchor motif;
519-549 2.49e-04

LPXTG cell wall anchor motif;


Pssm-ID: 366278 [Multi-domain]  Cd Length: 43  Bit Score: 38.68  E-value: 2.49e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446641959  519 LPVTGGIGTTLFTVIGLTLMLTAAFVFFRKK 549
Cdd:pfam00746   9 LPKTGENSNIFLTAAGLLALLGGLLLLVKRR 39
SdrD_B pfam17210
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This ...
178-272 1.17e-03

SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold.


Pssm-ID: 435789 [Multi-domain]  Cd Length: 112  Bit Score: 38.74  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  178 NEKALAGAVFSLFKKDGTEVKKElVTDANGHIRVQGLEYGEYYFQETkAPKGYVIDPtkreffvKNSG---TINEDGTIT 254
Cdd:pfam17210  20 GEPGISGVTVTLYDANGTVVGTT-TTDANGKYLFTNLAPGTYYVEFT-APAGYTFTP-------QNQGsddALDSDADPA 90
                          90
                  ....*....|....*....
gi 446641959  255 SGTVVKIEVKNNEE-PTID 272
Cdd:pfam17210  91 TGLTATVTLASGESdLTID 109
GramPos_pilinBB pfam16569
Gram-positive pilin backbone subunit 2, Cna-B-like domain; GramPos_pilinBB is one of the major ...
291-392 1.58e-03

Gram-positive pilin backbone subunit 2, Cna-B-like domain; GramPos_pilinBB is one of the major backbone units of Gram-positive pili, such as those from S.pneumoniae. There are three major pilin subunits that form the polymeric backbone of the pilin from S. pneumoniae, constructed of three transthyretin-like, CnaB, domains along with a crucial N-terminal domain, D1. The three Cna-B like domains are stabilized by internal Lys-Asn isopeptdie bonds, Gram-positive pili are formed from a single chain of covalently linked subunit proteins (pilins), usually comprising an adhesin at the distal tip, a major pilin that forms the polymer shaft and a minor pilin that mediates cell wall anchoring at the base.


Pssm-ID: 435436  Cd Length: 114  Bit Score: 38.53  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446641959  291 NYDIKTLIPEDiKEYKKYVVTDTLDNRLVIQGKPIVKIDGAEVNANVVEVAIEGQKVTATVKD--FTKLDGKK-----EF 363
Cdd:pfam16569   6 PYELTGKVPKN-AGYEKYVFTDTMSKGLTYNEDVKVKVGGTDVTDTDYTLAVDADTFTLTFTFanLKKFEKAKatagsEI 84
                          90       100
                  ....*....|....*....|....*....
gi 446641959  364 HLQIKSQVKEGVPSGSEILNTAKIHFTNK 392
Cdd:pfam16569  85 TVTYTATLNENAVIDNGNPNDAKLVYSNN 113
 
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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