ID   A0A099GCS7_9RHOB        Unreviewed;       613 AA.
AC   A0A099GCS7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:KGJ20519.1};
GN   ORFNames=IX56_13890 {ECO:0000313|EMBL:KGJ20519.1};
OS   Paracoccus sanguinis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1545044 {ECO:0000313|EMBL:KGJ20519.1, ECO:0000313|Proteomes:UP000029858};
RN   [1] {ECO:0000313|EMBL:KGJ20519.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ20519.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ20519.1, ECO:0000313|Proteomes:UP000029858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5503 {ECO:0000313|EMBL:KGJ20519.1,
RC   ECO:0000313|Proteomes:UP000029858};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of New
RT   York State patients.";
RL   Submitted (OCT-2014) 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|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:KGJ20519.1}.
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DR   EMBL; JRKQ01000091; KGJ20519.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A099GCS7; -.
DR   Proteomes; UP000029858; 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; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   NCBIfam; TIGR02290; M3_fam_3; 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|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029858};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          134..203
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          357..598
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  68480 MW;  BD0CD7791E31AFA1 CRC64;
     MTPRRPQMTR SRHFDAEQPG AAALDLGPLP EWDLSDLYTA PDAPEIKADL ARLDEATASF
     AADYEGRLAD LSPAEMLECI ERYQTIDLIA GRLMSYAGLR YYQNTTDAGR AKAMGDLQAK
     ITDMTTPLVF FSLEFNRIPD ATYEAVFAAA DGPARYKPVF DRMRAMRPHQ LSDELEKFLH
     DNSVVGAAAW NRLFDETTAA LTFDVDGETL GLEATLNLLT DHDRTRREAG ARALARVFTD
     NVKLFARIHN TLAKEKAIED KWRKMPTPQH GRHLSNHVEP EVVQALRDAV VAAYPRLSHR
     YYRLKARWLG LEKLQVWDRN APLPQETPRL IGWDEARTTV LDAYAGFDPE LAKLAEPFFD
     RGWIDAAVKP GKAPGAFAHP TVTDAHPFVL LNYLGKPRDV MTLAHELGHG VHQRLAAAQG
     ELLASTPLTL AETASVFGEM LTFRALLAKT TDPAQRKALL AGKVEDMINT VVRQIAFYDF
     ESRLHAARAE GELTPDDINA IWMTVQHESL GDAFDYMEGY ETFWAYIPHF IHSPFYVYAY
     AFGDGLVNAL YAAYEAAPEG FPARYFDLLK AGGSQHHSTL LQPFGLDAAD PAFWDKGLSM
     IEGFIDELEA MEG
//