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Database: UniProt
Entry: K9EEN5_9BACE
LinkDB: K9EEN5_9BACE
Original site: K9EEN5_9BACE 
ID   K9EEN5_9BACE            Unreviewed;       694 AA.
AC   K9EEN5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=HMPREF9447_05074 {ECO:0000313|EMBL:EKU87615.1};
OS   Bacteroides oleiciplenus YIT 12058.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=742727 {ECO:0000313|EMBL:EKU87615.1, ECO:0000313|Proteomes:UP000009872};
RN   [1] {ECO:0000313|EMBL:EKU87615.1, ECO:0000313|Proteomes:UP000009872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12058 {ECO:0000313|EMBL:EKU87615.1,
RC   ECO:0000313|Proteomes:UP000009872};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Walker B.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bacteroides oleiciplenus YIT 12058.";
RL   Submitted (SEP-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKU87615.1}.
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DR   EMBL; ADLF01000024; EKU87615.1; -; Genomic_DNA.
DR   RefSeq; WP_009132452.1; NZ_JH992946.1.
DR   AlphaFoldDB; K9EEN5; -.
DR   STRING; 742727.HMPREF9447_05074; -.
DR   PATRIC; fig|742727.4.peg.5184; -.
DR   eggNOG; COG0339; Bacteria.
DR   HOGENOM; CLU_001805_4_0_10; -.
DR   OrthoDB; 9773538at2; -.
DR   Proteomes; UP000009872; 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; 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; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..694
FT                   /note="Peptidase M3A/M3B catalytic domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003927382"
FT   DOMAIN          249..692
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   694 AA;  79343 MW;  9C30AB00DB943ABB CRC64;
     MFKKCIFILA TSCMMYSCAT QTETNPFLTE FQTEHGVPPF DKIKLEHYEP AFLKGIEEQN
     ANIDAIVNNS EAPTFENVIV AFDNSSPILD RVSAIFYNMT DAEKTDGLNE LSIKLAPTLS
     EHSDNISLNQ ELFKKVSAVY QQKESLGLTT EQQRLLEETY KDFVRSGANL SPEKQARLRE
     INKQLSTLGL KFSDNILNEN NAFKLYIDKE EDLAGLPDWF CQSAAEKAKE DGQEGKWLFT
     LGNASRIPFL QYSANRPLRE QMYKAYISRG NNNDKNDNKK IITDIVSLRL EKAQLLGFDC
     YSNFVLDNTM AKNSTTVMDF LNNLWSYSLP KAKAEAAELQ KIMDKDGKGE KLEGWDWWYY
     TEKLRKEKYN LEEDEIKPYF KLENVREGAF AVANKLYGIT LTKLEGIPVY HPDVEVFEVK
     DADGSHLGVF YVDYFPRPGK SGGAWMSNYR EQQGNIRPLV CNVCSFTQPV GDMPSLLTID
     EVETLFHEFG HALHGLLTKC NYKGISGTNV VRDFVELPSQ INEHWATEPE VLKMYAKHYQ
     TGETIPDSLI EKILNQKTFN QGFMTTELLA AAILDMNLHN LTDTKDLDVL AYEKEAMDQL
     GLIPEIAPRY RTTYFNHIIG GYAAGYYSYL WANVLDNDAF EAFKEHGIFD KKTADLFRYN
     VLEKGNSEDP MTLYKNFRGT EPQLEPMLKN RGMK
//
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