ID   C3QSK4_9BACE            Unreviewed;       686 AA.
AC   C3QSK4;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   SubName: Full=Putative oligopeptidase A {ECO:0000313|EMBL:EEO54938.1};
GN   ORFNames=BSCG_01863 {ECO:0000313|EMBL:EEO54938.1};
OS   Bacteroides sp. 2_2_4.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=469590 {ECO:0000313|EMBL:EEO54938.1};
RN   [1] {ECO:0000313|EMBL:EEO54938.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_2_4 {ECO:0000313|EMBL:EEO54938.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E.,
RA   Nusbaum C., Ilzarbe M., Galagan J., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. strain 2_2_4.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; EQ973358; EEO54938.1; -; Genomic_DNA.
DR   RefSeq; WP_004308572.1; NZ_EQ973358.1.
DR   AlphaFoldDB; C3QSK4; -.
DR   HOGENOM; CLU_001805_4_0_10; -.
DR   Proteomes; UP000003969; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 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; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          232..682
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   686 AA;  79368 MW;  567F8496057D0FED CRC64;
     MNNITNAQNP FYGQYHTPHE AVPFDRIETE HYEPAILEGI KLQNAEIEAI IQNPEKADFT
     NTIEAFEESG KLLDKVVAVF GNMLSAETND DLQELAQKIM PLLSEHSNNI TLNEKLFARV
     KEVYNQKETL QLTQEQKQLL ENAYNSFIRH GANLEGEARE EYRRLTTELS KLTLTFSENN
     LKETNAYQML LTKKESLAGL PEIIIEAAAE TAKNEEKEGW AFTLHAPSYI PFMTYSDNRD
     LRQKLYMAYN TKCTHDNEFN NIDIVKKIAN TRMKIAQLLG YKDYAEYTLK KRMAENSKSV
     YKLLNQLLEA YTPTAQQEYK EIQELAREEQ GADFVVMPWD WSYYSNKLKD KKFNINEEML
     RPYFELEQVK KGVFGLAEKL YGITFRKNTE IPVYHKEVEA FEVFDKDGKF LAVLYTDFHP
     RPGKRAGAWM TSYKDQWIDK KTGKNSRPHV SVVMNFTKPT ENKPALLTFN EVETFLHEFG
     HSLHGMFANS TYRSLSGTNV YWDFVELPSQ IMENFAIEKD FLNTFARHYQ TGEVLPDELI
     KRLVDASNFN VAYACLRQIS FGLLDMAWYT HNTPFEGDVK AYEQEAWKDA QILPVVQEAC
     MSTQFSHIFA GGYAAGYYSY KWAEVLDADA FSLFKQKGIF NQEVADSFRN NILSKGGTEH
     PMILYKRFRG QEPSIDALLI RNGIKK
//