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Conserved domains on  [gi|446650132|ref|WP_000727478|]
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MULTISPECIES: peptidylprolyl isomerase PrsA [Bacillus]

Protein Classification

peptidylprolyl isomerase PrsA( domain architecture ID 11479868)

peptidylprolyl isomerase PrsA plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins, and it functions as a peptidyl-prolyl cis-trans isomerase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  10228556

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 1-283 1.38e-157

peptidylprolyl isomerase; Reviewed


:

Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 440.18  E-value: 1.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   1 MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNVTEKELSKELKQKYGESTLYQMVLSKALLDKYKVSDEEATKQVKE 80
Cdd:PRK02998   1 MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNITEKELSKELRQKYGESTLYQMVLSKALLDKYKVSDEEAKKQVEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  81 AKDKMGDNFKETLEKLGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNGED 160
Cdd:PRK02998  81 AKDKMGDNFKSTLEQVGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNGED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 161 FAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKELKPFEEVKDKIRKDL 240
Cdd:PRK02998 161 FAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKKELKPFDEVKDSIRKDL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446650132 241 EQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEYKETFKFLEKK 283
Cdd:PRK02998 241 EQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEFKDTFKFLEKK 283
 
Name Accession Description Interval E-value
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 1-283 1.38e-157

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 440.18  E-value: 1.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   1 MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNVTEKELSKELKQKYGESTLYQMVLSKALLDKYKVSDEEATKQVKE 80
Cdd:PRK02998   1 MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNITEKELSKELRQKYGESTLYQMVLSKALLDKYKVSDEEAKKQVEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  81 AKDKMGDNFKETLEKLGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNGED 160
Cdd:PRK02998  81 AKDKMGDNFKSTLEQVGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNGED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 161 FAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKELKPFEEVKDKIRKDL 240
Cdd:PRK02998 161 FAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKKELKPFDEVKDSIRKDL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446650132 241 EQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEYKETFKFLEKK 283
Cdd:PRK02998 241 EQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEFKDTFKFLEKK 283
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 132-256 2.19e-44

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 147.41  E-value: 2.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 132 KPEMKVSHILV---------KDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNA 202
Cdd:COG0760    6 PEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446650132 203 GQVSEPVKTSYGYHIIKVTDKKE--LKPFEEVKDKIRKDLEQQRLQDTTGKWKQQV 256
Cdd:COG0760   86 GEISGPVKTQFGYHIIKVEDRRPaeTPPFEEVKQQIRQELFQQALEAWLEELRKKA 141
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 136-224 3.78e-27

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 101.67  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  136 KVSHILV-------KDEKTAK----EVKEKVNNGEDFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQ 204
Cdd:pfam13616  17 KASHILIsysqavsRTEEEAKakadSLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQMVKEFEDAVFSLKVGE 96

                          90       100
                  ....*....|....*....|
gi 446650132  205 VSEPVKTSYGYHIIKVTDKK 224
Cdd:pfam13616  97 ISGVVKTQFGFHIIKVTDKK 116
 
Name Accession Description Interval E-value
prsA PRK02998
peptidylprolyl isomerase; Reviewed
 1-283 1.38e-157

peptidylprolyl isomerase; Reviewed


Pssm-ID: 179522 [Multi-domain]  Cd Length: 283  Bit Score: 440.18  E-value: 1.38e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   1 MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNVTEKELSKELKQKYGESTLYQMVLSKALLDKYKVSDEEATKQVKE 80
Cdd:PRK02998   1 MKKKKLFLGTIISCVVLALSACGSSDNVVTSKVGNITEKELSKELRQKYGESTLYQMVLSKALLDKYKVSDEEAKKQVEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  81 AKDKMGDNFKETLEKLGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNGED 160
Cdd:PRK02998  81 AKDKMGDNFKSTLEQVGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNGED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 161 FAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKELKPFEEVKDKIRKDL 240
Cdd:PRK02998 161 FAALAKQYSEDTGSKEQGGEISGFAPGQTVKEFEEAAYKLDAGQVSEPVKTTYGYHIIKVTDKKELKPFDEVKDSIRKDL 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 446650132 241 EQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEYKETFKFLEKK 283
Cdd:PRK02998 241 EQQRLQDTTGKWKQQVVNDLLKDADIKVNDKEFKDTFKFLEKK 283
prsA PRK03002
peptidylprolyl isomerase PrsA;
1-283 2.01e-84

peptidylprolyl isomerase PrsA;


Pssm-ID: 101162 [Multi-domain]  Cd Length: 285  Bit Score: 254.47  E-value: 2.01e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   1 MKKKKLFLGTIIsCVVLALSACG---SSDNVVTSKVGNVTEKELSKELKQKYGESTLYQMVLSKALLDKYKVSDEEATKQ 77
Cdd:PRK03002   1 MRGKHIFIITAL-ISILMLSACGqknSSATVATATDSTITKSDFEKQLKDRYGKDMLYEMMAQDVITKKYKVSDDDVDKE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  78 VKEAKDKMGDNFKETLEKLGLKNEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNN 157
Cdd:PRK03002  80 VQKAKSQYGDQFKNVLKNNGLKDEADFKNQIKFKLAMNEAIKKSVTEKDVKDHYKPEIKASHILVSDENEAKEIKKKLDA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 158 GEDFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKELKPFEEVKDKIR 237
Cdd:PRK03002 160 GASFEELAKQESQDLLSKEKGGDLGYFNSGRMAPEFETAAYKLKVGQISNPVKSPNGYHIIKLTDKKDLKPYDEVKDSIR 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446650132 238 KDLEQQRLQDTTgkWKQQVVNDLLKDADIKVNDKEYKETFKFLEKK 283
Cdd:PRK03002 240 KNLEEERTADPI--FGKKLLQSELKKANIKINDSELEDTFTIVSPQ 283
prsA PRK03095
peptidylprolyl isomerase PrsA;
1-278 3.99e-69

peptidylprolyl isomerase PrsA;


Pssm-ID: 179537 [Multi-domain]  Cd Length: 287  Bit Score: 215.63  E-value: 3.99e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   1 MKKKKLFLGtiiSCVVLALSACG--SSDNVVTSKVGNVTEKELSKELKQKYGESTLYQMVLSKALLDKYKVSDEEATKQV 78
Cdd:PRK03095   1 MKKAMLALA---ATSVIALSACGtsSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYKVEDKEVDKKY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  79 KEAKDKMGDNFKETLEKLGLKnEDELKEKMKPEIAFEKAIKATVTEKDVKDNYKPEMKVSHILVKDEKTAKEVKEKVNNG 158
Cdd:PRK03095  78 DEMKKQYGDQFDTLLKQQGIK-EETLKTGVRAQLAQEKAIEKTITDKELKDNYKPEIKASHILVKDEATAKKVKEELGQG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 159 EDFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKEL-KPFEEVKDKIR 237
Cdd:PRK03095 157 KSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPeKSFEQSKADIK 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446650132 238 KDLEQQRLQDttGKWKQQVVNDLLKDADIKVNDKEYKETFK 278
Cdd:PRK03095 237 KELVQKKAQD--GEFMNDLMMKEIKKADVKVDDKDLKDLFE 275
SurA COG0760
Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, ...
 132-256 2.19e-44

Peptidyl-prolyl isomerase, parvulin family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440523 [Multi-domain]  Cd Length: 143  Bit Score: 147.41  E-value: 2.19e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 132 KPEMKVSHILV---------KDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNA 202
Cdd:COG0760    6 PEEVRASHILVkvppsedraKAEAKAEELLAQLKAGADFAELAKEYSQDPGSAANGGDLGWFSRGQLVPEFEEAAFALKP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446650132 203 GQVSEPVKTSYGYHIIKVTDKKE--LKPFEEVKDKIRKDLEQQRLQDTTGKWKQQV 256
Cdd:COG0760   86 GEISGPVKTQFGYHIIKVEDRRPaeTPPFEEVKQQIRQELFQQALEAWLEELRKKA 141
prsA PRK04405
peptidylprolyl isomerase; Provisional
 1-274 2.21e-40

peptidylprolyl isomerase; Provisional


Pssm-ID: 235295 [Multi-domain]  Cd Length: 298  Bit Score: 141.84  E-value: 2.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   1 MKK--KKLFLGTIISCVVLALSACGSSDN-VVTSKVGNVTEKELSKELKQ-KYGESTLYQMVLSKALLDKY--KVSDEEA 74
Cdd:PRK04405   1 MKKkmKKWALAAASAGLALSLAGCSSNQAtVATYSGGKITQSQYYKEMKQsSAGKTVLANMIIYRALEKQYgkKVSTKKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  75 TKQVKEAKDKMGDNFKETLEKLGLkNEDELKEKMKPEIAFEKAIKA--TVTEKDVKD---NYKPEMKVSHILVKDEKTAK 149
Cdd:PRK04405  81 DKQYNSYKKQYGSSFDSVLSQNGM-TTSSFKQNLRTNLLSEAALKKlkKVTNSQLKKawkSYQPKVTVQHILVSKKSTAE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 150 EVKEKVNNGEDFAALAKQYSEDTGSKEQGGEIAGFGPGQTV--KEFEEAAYKLNAGQV-SEPVKTSYGYHIIKVTDKKEL 226
Cdd:PRK04405 160 TVIKKLKDGKDFAKLAKKYSTDTATKNKGGKLSAFDSTDTTldSTFKTAAFKLKNGEYtTTPVKTTYGYEVIKMIKHPAK 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 446650132 227 KPFEEVKDKIRKDLEQQRLQDTTGkwKQQVVNDLLKDADIKVNDKEYK 274
Cdd:PRK04405 240 GTFSDHKKALTKQIYAKWASDSSV--MQRVISKVLKKANVSIKDKDLK 285
prsA PRK00059
peptidylprolyl isomerase; Provisional
 39-271 1.00e-33

peptidylprolyl isomerase; Provisional


Pssm-ID: 234605 [Multi-domain]  Cd Length: 336  Bit Score: 125.21  E-value: 1.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  39 KELSKELKQKYGESTLYQ-MVLSKALLDKYKVSDEEATKQV-------KEAKDKMGDNFKETLEKLGLkNEDELKEKMKP 110
Cdd:PRK00059  79 KEQIKQQKEQILDSLITEkVLLQKAKELKLIPSEEELNKEVdkkineiKKQFNNDEEQFEEALKATGF-TEETFKEYLKN 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 111 EIAFEKAIK-----ATVTEKDVKDNY----------KPEMKVSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSK 175
Cdd:PRK00059 158 QIIIEKVINevvkdVKVTDKDAQKYYnenkskftekPNTMHLAHILVKTEDEAKKVKKRLDKGEDFAKVAKEVSQDPGSK 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 176 EQGGEI--AGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKE--LKPFEEVKDKIRKDLEQQR----LQD 247
Cdd:PRK00059 238 DKGGDLgdVPYSDSGYDKEFMDGAKALKEGEISAPVKTQFGYHIIKAIKKKEypVKPFDSVKEDIKKQLLQEKqsevFKK 317

                        250       260
                 ....*....|....*....|....
gi 446650132 248 TTGKWKqqvvndllKDADIKVNDK 271
Cdd:PRK00059 318 KIEEWK--------KALKVKKYEK 333
Rotamase_3 pfam13616
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 136-224 3.78e-27

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 404499 [Multi-domain]  Cd Length: 116  Bit Score: 101.67  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  136 KVSHILV-------KDEKTAK----EVKEKVNNGEDFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQ 204
Cdd:pfam13616  17 KASHILIsysqavsRTEEEAKakadSLLAALKNGADFAALAKTYSDDPASKNNGGDLGWFTKGQMVKEFEDAVFSLKVGE 96

                          90       100
                  ....*....|....*....|
gi 446650132  205 VSEPVKTSYGYHIIKVTDKK 224
Cdd:pfam13616  97 ISGVVKTQFGFHIIKVTDKK 116
prsA PRK01326
foldase protein PrsA; Reviewed
 2-277 3.53e-26

foldase protein PrsA; Reviewed


Pssm-ID: 179281 [Multi-domain]  Cd Length: 310  Bit Score: 104.51  E-value: 3.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   2 KKKKLFLGTIISCVVLALSACGSSD---NVVTSKVGNVTEKELSKELKQ-KYGESTLYQMVLSKALLDKY--KVSDEEAT 75
Cdd:PRK01326   1 MKKKLIAGAVTLLSVATLAACSKTNentKVISMKGDTITVSDFYNQVKNnPSAQQAMLNLTISRVFEKQYgdKVSDKEVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  76 KQVKEAKDKMGDNFKETLEKLGLKNED---ELKEKMKPEIAFEKAIKATVTEKDVK---DNYKPEMKVSHILVKDEKTAK 149
Cdd:PRK01326  81 KAYAKTAKQYGASFSRALAQAGLTPETykaQIRTSKLVEYAVKEAAKKELTDEAYKkayEEYTPEVTAQIIRLDNEDKAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 150 EVKEKVN-NGEDFAALAKqysEDTGSKEQGGEIAgFGPGQTV--KEFEEAAYKLNAGQVSEPVKT------SYGYHIIKV 220
Cdd:PRK01326 161 SVLEEAKaEGADFAQIAK---ENTTTKEKKGEYK-FDSGSTNvpEQVKKAAFALDEDGVSDVISVldptayQSKYYIVKV 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446650132 221 TDKKELKP-FEEVKDKIRKDLEQQRLQDTTgkWKQQVVNDLLKDADIKVNDKEYKETF 277
Cdd:PRK01326 237 TKKTEKKSdWKDYKKRLKAIILAQKQNDSN--FQNKVIAKALDKANVKIKDKAFANIL 292
Rotamase pfam00639
PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the ...
 139-222 2.78e-25

PPIC-type PPIASE domain; Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline.


Pssm-ID: 425792 [Multi-domain]  Cd Length: 96  Bit Score: 96.21  E-value: 2.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  139 HILVK-DEKT----------AKEVKEKVNNGED-FAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVS 206
Cdd:pfam00639   1 HILIKtPEASerdraeakakAEEILEQLKSGEDsFAELARKYSDDCPSAANGGDLGWFTRGQLPPEFEKAAFALKPGEIS 80

                          90
                  ....*....|....*.
gi 446650132  207 EPVKTSYGYHIIKVTD 222
Cdd:pfam00639  81 GPVETRFGFHIIKLTD 96
PRK10788 PRK10788
periplasmic folding chaperone; Provisional
 119-256 6.52e-20

periplasmic folding chaperone; Provisional


Pssm-ID: 182731 [Multi-domain]  Cd Length: 623  Bit Score: 89.30  E-value: 6.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 119 KATVTEKDVKDNYK--------PEMK-VSHILVKDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKEQGGEIAGFGPGQT 189
Cdd:PRK10788 246 KITVSDADIQAYYDqhqdqftqPERKrYSIIQTKTEAEAKAVLDELKKGADFATLAKEKSTDIISARNGGDLGWLEPATT 325

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446650132 190 VKEFEEAAYKlNAGQVSEPVKTSYGYHIIKVTDKK--ELKPFEEVKDKIRKDLEQQRLQDTTGKWKQQV 256
Cdd:PRK10788 326 PDELKNAGLK-EKGQLSGVIKSSVGFLIVRLDDIQpaKVKPLSEVRDDIAAKVKQEKALDAYYALQQKV 393
PRK12450 PRK12450
foldase protein PrsA; Reviewed
 2-273 4.86e-17

foldase protein PrsA; Reviewed


Pssm-ID: 138982 [Multi-domain]  Cd Length: 309  Bit Score: 79.36  E-value: 4.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132   2 KKKKLFLGTIISCVVLALSACGSSDN---VVTSKVGNVTEKELSKELKQ-KYGESTLYQMVLSKALLDKY--KVSDEEAT 75
Cdd:PRK12450   3 QMNKLITGVVTLATVVTLSACQSSHNntkLVSMKGDTITVSDFYNETKNtELAQKAMLSLVISRVFETQYanKVSDKEVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  76 KQVKEAKDKMGDNFKETLEKLGLKNED---ELKEKMKPEIAF-EKAIKATVTEKDVK---DNYKPEMKVSHILVKDEKTA 148
Cdd:PRK12450  83 KAYKQTADQYGTSFKTVLAQSGLTPETykkQIRLTKLVEYAVkEQAKNETISKKDYRqayDAYTPTMTAEIMQFEKEEDA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 149 KEVKEKVN-NGEDFAALAKQYSEDTGSKEQggeiAGFGPGQTV--KEFEEAAYKLNAGQVSE------PVKTSYGYHIIK 219
Cdd:PRK12450 163 KAALEAVKaEGADFAAIAKEKTIAADKKTT----YTFDSGETTlpAEVVRAASGLKEGNRSEiitaldPATSKRTYHIIK 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446650132 220 VTDKKELKP-FEEVKDKIRKDLEQQRLQDTtgKWKQQVVNDLLKDADIKVNDKEY 273
Cdd:PRK12450 239 VTKKATKKAdWKAYQKRLKDIIVTGKLKDP--DFQNKVIAKALDKANVKIKDKAF 291
PTZ00356 PTZ00356
peptidyl-prolyl cis-trans isomerase (PPIase); Provisional
 136-219 4.04e-15

peptidyl-prolyl cis-trans isomerase (PPIase); Provisional


Pssm-ID: 185573 [Multi-domain]  Cd Length: 115  Bit Score: 70.05  E-value: 4.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 136 KVSHILVK--------DEKTAKEV--------------KEKVNNGE-DFAALAKQYSeDTGSKEQGGEIAGFGPGQTVKE 192
Cdd:PTZ00356   7 RAAHLLIKhtgsrnpvSRRTGKPVtrskeeaikelakwREQIVSGEkTFEEIARQRS-DCGSAAKGGDLGFFGRGQMQKP 85

                         90       100
                 ....*....|....*....|....*..
gi 446650132 193 FEEAAYKLNAGQVSEPVKTSYGYHIIK 219
Cdd:PTZ00356  86 FEDAAFALKVGEISDIVHTDSGVHIIL 112
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 134-255 9.48e-14

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 70.54  E-value: 9.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 134 EMKVSHILVK-------DEKTAK--EVKEKVNNGE-DFAALAKQYSEDTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAG 203
Cdd:PRK10770 266 EVHARHILLKpspimtdEQARAKleQIAADIKSGKtTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALMRLNKG 345

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446650132 204 QVSEPVKTSYGYHIIKVTDKKEL-KPFEEVKDKIRKDLEQQRLQDTTGKWKQQ 255
Cdd:PRK10770 346 QISAPVHSSFGWHLIELLDTRQVdKTDAAQKDRAYRMLFNRKFSEEAQTWMQE 398
PRK15441 PRK15441
peptidyl-prolyl cis-trans isomerase C; Provisional
 139-224 4.10e-13

peptidyl-prolyl cis-trans isomerase C; Provisional


Pssm-ID: 185338 [Multi-domain]  Cd Length: 93  Bit Score: 63.89  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 139 HILVKDEKTAKEVKEKVNNGEDFAALAKQYSEdTGSKEQGGEIAGFGPGQTVKEFEEAAYKLNAGQVSEPVKTSYGYHII 218
Cdd:PRK15441   9 HILVKEEKLALDLLEQIKNGADFGKLAKKHSI-CPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHII 87


                 ....*.
gi 446650132 219 KVTDKK 224
Cdd:PRK15441  88 KVLYRN 93
Rotamase_2 pfam13145
PPIC-type PPIASE domain;
122-234 2.67e-12

PPIC-type PPIASE domain;


Pssm-ID: 432992 [Multi-domain]  Cd Length: 121  Bit Score: 62.46  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132  122 VTEKDVKDNY--------KPEMKVSHILVKDEKTAKEVKEKV---NNGEDFAALAKQYSEDTGSKEQGGEIAGFGPgqtv 190
Cdd:pfam13145   1 VTEEELKAYYeenkdefsTPEGRLLEILVFKDQVAADAALALlkaGALEDFAALAKGEGIKAATLDIVESAELLPE---- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446650132  191 kEFEEAAYKLNAGQVSEPVKTSYGYHIIKVTDKKE--LKPFEEVKD 234
Cdd:pfam13145  77 -ELAKAAFALKPGEVSGPIKTGNGYYVVRVTEIKPaqPLPFEEAKD 121
PRK10770 PRK10770
peptidyl-prolyl cis-trans isomerase SurA; Provisional
 133-222 1.20e-07

peptidyl-prolyl cis-trans isomerase SurA; Provisional


Pssm-ID: 236758 [Multi-domain]  Cd Length: 413  Bit Score: 52.44  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446650132 133 PEMKVSHILV------------KDEKTAKEVKEKVNNGEDFAALAKQYSEDTGSKeQGGEIaGFGPGQTVKE-FEEAAYK 199
Cdd:PRK10770 154 TELNLSHILIplpenptqdqvdEAESQARSIVDQARNGADFGKLAIAYSADQQAL-KGGQM-GWGRIQELPGlFAQALST 231

                         90       100
                 ....*....|....*....|...
gi 446650132 200 LNAGQVSEPVKTSYGYHIIKVTD 222
Cdd:PRK10770 232 AKKGDIVGPIRSGVGFHILKVND 254
BamE COG2913
Outer membrane protein assembly factor BamE, lipoprotein component of the BamABCDE complex ...
 1-46 9.84e-03

Outer membrane protein assembly factor BamE, lipoprotein component of the BamABCDE complex [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442157  Cd Length: 128  Bit Score: 35.40  E-value: 9.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446650132   1 MKKKKLFLgtIISCVVLALSACGSSDNVVTSKVGNVTEKELSKELK 46
Cdd:COG2913    1 MRKLRLLL--LALLLALLLAGCSSFVYKIDIQQGNVVTQEDLAQLK 44
 
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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