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
//