ID C4LD59_TOLAT Unreviewed; 679 AA.
AC C4LD59;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=oligopeptidase A {ECO:0000256|ARBA:ARBA00026100};
DE EC=3.4.24.70 {ECO:0000256|ARBA:ARBA00026100};
GN OrderedLocusNames=Tola_3001 {ECO:0000313|EMBL:ACQ94590.1};
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494 {ECO:0000313|EMBL:ACQ94590.1, ECO:0000313|Proteomes:UP000009073};
RN [1] {ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACQ94590.1, ECO:0000313|Proteomes:UP000009073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4 {ECO:0000313|Proteomes:UP000009073};
RX PubMed=22180815; DOI=10.4056/sigs.2184986;
RA Chertkov O., Copeland A., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA Bruce D., Goodwin L., Han C., Tapia R., Saunders E., Schmutz J.,
RA Brettin T., Larimer F., Land M., Hauser L., Spring S., Rohde M.,
RA Kyrpides N.C., Ivanova N., Goker M., Beller H.R., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Tolumonas auensis type strain (TA 4).";
RL Stand. Genomic Sci. 5:112-120(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of oligopeptides, with broad specificity. Gly or
CC Ala commonly occur as P1 or P1' residues, but more distant residues
CC are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-
CC Pro-Ala is cleaved, but not Z-(Gly)(5).; EC=3.4.24.70;
CC Evidence={ECO:0000256|ARBA:ARBA00024603};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR EMBL; CP001616; ACQ94590.1; -; Genomic_DNA.
DR RefSeq; WP_015880039.1; NC_012691.1.
DR AlphaFoldDB; C4LD59; -.
DR STRING; 595494.Tola_3001; -.
DR MEROPS; M03.004; -.
DR KEGG; tau:Tola_3001; -.
DR eggNOG; COG0339; Bacteria.
DR HOGENOM; CLU_001805_4_1_6; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000009073; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045666; OpdA_N.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR Pfam; PF19310; TOP_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000009073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 41..148
FT /note="Oligopeptidase A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19310"
FT DOMAIN 222..677
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 679 AA; 77219 MW; 8D8FD20D2953650F CRC64;
MSNPLLSMDG LPPFSKIKPE HVQPAVQQAI GEAKQRIADV LRSSDNLTWD SLIAPLEESD
DRLSRIWSPV SHMNSVVNND ELRAAYETCL PLLSEYQTFV GQNAGLYSAY QQLAESNDFR
RLSQAQQQQV NNTLRDFRLS GIALPAEQQQ RYGQIVSRLS ELASQFNNQV MDATQAWIKQ
ITDEAELAGL PDSAKAAARQ QAQSRELEGW VFTLDIPSYL PLMMYADSRA LREEAYTAFT
TRASDQGPDA GKWDNSPLIE EILALRHELA QLLGFANYAE RSLATKMAHS TEQVIDFLSD
LAARSRPHAQ RELQELQAFA QKEHGIETLA AWDIAYYSEK LKQHLYAISN EMLRPYFPEH
KVIQGLFEVV KRLFGMRIKP HLAVETWHPD VRFYDIVDAD GELRGSFYLD LYARAKKRGG
AWMDDCMGRR YRRDGQLQHP VAYLTCNFNG PVEGKPALFT HDEVVTLFHE FGHGLHHMLT
QIDVAGVAGI NGVPWDAVEL PSQFLENWCW EPEALAVISG HYETGEPLPK SELDKLLAAK
NFQSAMQMVR QLEFALFDFR LHREYDPQQG GRVQQILDEV RQQVAVMMPP AFNRFQHSFS
HIFGGGYAAG YYSYKWAEVL SADAFSRFEE EGIFNPQTGR DFLQYILEKG GSEEPMTLFK
AFRGREPKID ALLRHCGIQ
//
