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Database: UniProt
Entry: A3TX13_PSEBH
LinkDB: A3TX13_PSEBH
Original site: A3TX13_PSEBH 
ID   A3TX13_PSEBH            Unreviewed;       606 AA.
AC   A3TX13;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:EAQ03373.1};
GN   ORFNames=OB2597_02097 {ECO:0000313|EMBL:EAQ03373.1};
OS   Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS   HTCC2597) (Oceanicola batsensis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ03373.1, ECO:0000313|Proteomes:UP000004318};
RN   [1] {ECO:0000313|EMBL:EAQ03373.1, ECO:0000313|Proteomes:UP000004318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597
RC   {ECO:0000313|Proteomes:UP000004318};
RX   PubMed=20418400; DOI=10.1128/JB.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
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|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:EAQ03373.1}.
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DR   EMBL; AAMO01000004; EAQ03373.1; -; Genomic_DNA.
DR   RefSeq; WP_009804673.1; NZ_CH724131.1.
DR   AlphaFoldDB; A3TX13; -.
DR   STRING; 252305.OB2597_02097; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_3_0_5; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000004318; 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; cd09610; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_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:UP000004318};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          128..196
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          211..591
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   606 AA;  68446 MW;  87CA1DB02476B82D CRC64;
     MTAHPAPLFD ANATSGGRDL GKLPEWDLTD LYASPEDPAI ERDLDWLREA CASFAADYEG
     KLDQLDAEGM LTCIRRDEEL TTVSGRLMSY AGLRYYQVTT DGARAKFMSD MQDRITTYTT
     PLVFFTLELN RLPDDRLDSL FAASDDLARY KPIFDRIRAM KPYQLSDEME KFLHDMGVVG
     DAWEKLFDET VAGLTFTIDG EELGLEATTT LLTEPDRDKR EAAAREIARV LGANIRTFAR
     VHNTQAKEKE VMDRWRGMPS AQTARHLSNH VEPEVVEALR NAVVAAYPRL SHRYYELKRK
     WLGLDRMQVW DRNAPLPIEP PRTVDWDTAQ EMVMSAYAGF DPRMANLAEP FFTRGWIDAG
     VKPGKAPGAF AHPTVTTVHP YVMLNYLGKP RDVMTLAHEL GHGVHQVLAA DQGELLSSTP
     LTLAETASVF GEMLTFRKLL DEAKSDAERK TLLAGKVEDM INTVVRQIAF YDFECKLHAA
     RREGELTPED INAIWMSVQA ESLGPAFDFM DGYEVFWSYI PHFIHSPFYV YAYAFGDGLV
     NALYAAYQEA PEGFQDKYFD MLRAGGSKHH KELLAPFGLD ASDPKFWDKG LSMIEGFIDE
     LEAMED
//
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