1BOQ,1GBD,1HPG,1P01,1P09,1QQ4,2EA3,2LPR,2OUA,2PFE,3M7U,3URC,4PRO,5MRR,5MRT,2H5C,2SFA,1SGC,2SGA,5SGA,1CSO,2GKV,1SGP


Conserved Protein Domain Family
alphaLP-like

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cd21112: alphaLP-like 
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins
This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.
Statistics
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PSSM-Id: 411050
Aligned: 464 rows
Threshold Bit Score: 84.2798
Threshold Setting Gi: 1400474897
Created: 23-Dec-2019
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
 
catalytic sitepeptidepro domain
Conserved site includes 3 residues -Click on image for an interactive view with Cn3D
Feature 1: catalytic site [active site], 3 residue positions
Conserved feature residue pattern:H D SClick to see conserved feature residue pattern help
Evidence:
  • Comment:Serine proteases contain the catalytic triad histidine, aspartate, and serine
  • Structure:2PFE: Thermobifida fusca Protease A (TFPA) in complex with an irreversible serine protease inhibitor (4-(2-aminoethyl)benzenesulfonyl fluoride); contacts at 4A
    View structure with Cn3D
  • Structure:1P01: Lysobacter enzymogenes alpha-lytic protease in complex with N-tert-butyloxycarbonylalanylprolylvaline boronic acid; contacts at 4.0A
    View structure with Cn3D
  • Citation:PMID 3122831

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                   #                                    
1BOQ_A         3 IVGGIEYSinn-------asLCSVGFSVtrg---atKGFVTAGHCGTVNATARigg---------avVGTFAARVFpg-- 61  Lysobacter enzy...
2PFE_A         3 IIGGNPYYfg--------nyRCSIGFSVrqg---sqTGFATAGHCGSTGTRVSs------------pSGTVAGSYFpg-- 57  Thermobifida fu...
WP_020519290  96 LRGGQAMNsyd-------grPCTTGLVTqyg---stFYLITAGHCLIGAQSPWwgeg-------gamIGPAHSATFpg-- 156 Catelliglobosis...
ERS41962     240 LAQGKSLYgpgtplfvgdsgVCTLAVAGtda--qgrKVGITAGHCGREGEYVA--------------SGDSWQVGN---- 299 Corynebacterium...
AGZ45002     146 TRGGVLLEgqsg----gsyyHCTATVLGtvsg-spaNATLTAGHCFDQSAPVYagrsnp--eiggyqLGTVSSRRFsg-- 216 Actinoplanes fr...
CEJ82719     102 LAHGRAQAed---------lAKQAGVSAsefgvkieDEIPTLMSSVRGGDIYHidsk------haysVGFSVNGGFisaa 166 Torrubiella hem...
WP_051104772  66 ARGGWGLTnpf-------aaPCTAGFAMkav--ngfNYIVTAGHCVADGMGTQwnla-------gylLGPGHFHSFpg-- 127 Catelliglobosis...
WP_051831019 122 AHGGRATVv-----------RHSLAVLNrak--dalDRASAAAVPAATPLWYVdvrs------ntlvVRSTDTARTetfl 182 Streptomyces no...
WP_089315258  14 IPPGGRVKir--------pdRVRGAAMTma-----aSGLVAAALAAAPAADATle----------ppAGRAAAPSDt--- 67  Actinomadura me...
WP_117210685 109 IYGGMAMDtay------lerRCSTGFLAqgg---gwYFLLTAGHCVANTSGSAavwyteggynsgglIGVRTTRPYyp-- 177 Micromonosporac...
Feature 1             #                                                                          
1BOQ_A        62 ----nDRAWVSLTs-------aQTLLPRVANgss------fvTVRGSTEAAVGAAVCRSGRt--tGYQCGTITAKniTAN 122 Lysobacter enzy...
2PFE_A        58 ----rDMGWVRITs-------aDTVTPLVNRyng-----gtvTVTGSQEAATGSSVCRSGAt--tGWRCGTIQSKnqTVR 119 Thermobifida fu...
WP_020519290 157 ----sDFGLLRVSdv-----spLTPRSEVAFqtg------yaRIGGVADVAVGTSVCKTGRt--tGTTCGTVLAKnaTYH 219 Catelliglobosis...
ERS41962     300 -----SGTIVASNe--------RHDYSVIEFgs-------naEVTRSYNNVTIDEIADGPHfgeqVCKNGVATGY--TCG 357 Corynebacterium...
AGZ45002     217 ---nvDAEAIRWSt-------gNTAYNYLNNcvyiy-ssdcrRITGGGGGSVGMAVQKSGIt--tGITSGTLTRLnvSVN 283 Actinoplanes fr...
CEJ82719     167 hcvkkGINVTDIEgnllgtaveSSFGGEVDSs----------YIKTIDGTNLTGYVNSYGQa---HFHCGTITAKnvTID 233 Torrubiella hem...
WP_051104772 128 ----nDYGVIMVAyn-----spVTTHPTLINyng-----sgvRVLGTNTPTIGQRLCKSGNv--sGVTCGTVLALdvTVT 191 Catelliglobosis...
WP_051831019 183 rqsgiDRALIRVEe--------VRAVPRPLAd----------LRGGDAFYIDGAARCSIGFpvpqGGQPGFVEERnaTVN 244 Streptomyces no...
WP_089315258  68 -----GGAAAKLV---------RRLGVTVDGrf--------rDITGAAGATVGETVTSSGSt--tGVHDGQVTALdqTVN 123 Actinomadura me...
WP_117210685 178 ---gdDFANIQISri-----tpHQYAPSVLHhgsprpvrgvgTARPPQDFFPGSPVCKTGRt--tGTTCGFVTRVnvSVT 247 Micromonosporac...
Feature 1                                 #                                                      
1BOQ_A       123 YA--EGAVrg---lTQGNACMGRGDSGGsWITs--------aGQAQGVMSGGnvqs-ngnnCGIpas---qrSSLFErl- 184 Lysobacter enzy...
2PFE_A       120 YA--EGTVtg---lTRTTACAEGGDSGGpWLTg---------SQAQGVTSGGtg------dCRSg------gITFFQpi- 172 Thermobifida fu...
WP_020519290 220 FQ--QGVVyg---lIETDACTAAGDSGApLIStrggygsrskYGAFGILSGSng-----vaCDGpg-----hRSAFQpl- 283 Catelliglobosis...
ERS41962     358 IH--YGAVqg---iQFNQVCASLGDSGGpLLTg---------NRLVGVISGGanptgldlsCRSplqgfvhvPTMATdan 423 Corynebacterium...
AGZ45002     284 VAdeDGTVtqltnqFETTACVIPGDSGGpLFSg---------GLLLGISSSVggln-ssgnCTSs------tRSYFSti- 346 Actinoplanes fr...
CEJ82719     234 FDfrHPSTg----lTETDVCAEPGDSGGsFFSg---------DQAQGTLSGGsg------eCARngps-kkgQQYFPpi- 292 Torrubiella hem...
WP_051104772 192 YH--TGEVvn--glIETAICASPGDSGSpLFRdpg----drrLIGMGVLSGGng-----vrCGDpg-----vRTYYNpl- 252 Catelliglobosis...
WP_051831019 245 YQ--EGSVyg---lTRTSVCAEPGDSGGsFVSg---------DQAQGVTSGGsg------dCTSg------gETYFQpv- 297 Streptomyces no...
WP_089315258 124 YQ--EGSVsg---lIQTTVCAEPGDSGGpLFAg---------SSAVGLTSGGsg------dCSSg------gVTFFQpm- 176 Actinomadura me...
WP_117210685 248 YH--DGVVsg---lIESSVCAGPGDSGGpLYGnd-------vTYAYGIVSGGns-----fpCGTsg-----fRSYHQpv- 304 Micromonosporac...
Feature 1                  
1BOQ_A       185 --qPILSQYG 192 Lysobacter enzymogenes
2PFE_A       173 --nPLLSYFG 180 Thermobifida fusca YX
WP_020519290 284 --pPVMSYYG 291 Catelliglobosispora koreensis
ERS41962     424 tlfADLNARG 433 Corynebacterium sp. KPL1995
AGZ45002     347 --nASMQAVG 354 Actinoplanes friuliensis DSM 7358
CEJ82719     293 --nKSLEAFN 300 Torrubiella hemipterigena
WP_051104772 253 --tEIMAAYG 260 Catelliglobosispora koreensis
WP_051831019 298 --nPILGTYG 305 Streptomyces novaecaesareae
WP_089315258 177 --tEPLSAFG 184 Actinomadura mexicana
WP_117210685 305 --rEALTAYG 312 Micromonosporaceae bacterium CPCC 204380

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