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Database: UniProt
Entry: J5PV71_9RHOB
LinkDB: J5PV71_9RHOB
Original site: J5PV71_9RHOB 
ID   J5PV71_9RHOB            Unreviewed;       610 AA.
AC   J5PV71;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:EJW13517.1};
GN   ORFNames=A33M_3501 {ECO:0000313|EMBL:EJW13517.1};
OS   Rhodovulum sp. PH10.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW13517.1, ECO:0000313|Proteomes:UP000002930};
RN   [1] {ECO:0000313|EMBL:EJW13517.1, ECO:0000313|Proteomes:UP000002930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PH10 {ECO:0000313|EMBL:EJW13517.1,
RC   ECO:0000313|Proteomes:UP000002930};
RX   PubMed=23105089; DOI=10.1128/JB.01695-12;
RA   Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT   "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT   Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT   India.";
RL   J. Bacteriol. 194:6363-6363(2012).
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:EJW13517.1}.
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DR   EMBL; AKZI01000007; EJW13517.1; -; Genomic_DNA.
DR   RefSeq; WP_008382517.1; NZ_AKZI01000007.1.
DR   AlphaFoldDB; J5PV71; -.
DR   STRING; 1187851.A33M_3501; -.
DR   PATRIC; fig|1187851.3.peg.195; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000002930; 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:UP000002930};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          130..198
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          213..592
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   610 AA;  67692 MW;  DE3062E2E0A1B6B3 CRC64;
     MADSPARTAP KKTEAALGAL PEWNLADLYP AIDSPEVRGD LARARAECIA FEEKYKGRLA
     EMAAAADAGK TLAEAVEGLE TLDDLLGRLI SYAGLVHAGD TTDPVRAKFY GDVQEQITAA
     SSHLLFFSLE LNRIDDALLE TAMGDPALGH YRPFIEDVRK EKPYQLEDRV EQLFHEKSVT
     GYAAWNRLFD ETVAGLRFKV QGKTLPLEPA LTLLQSPNEK TRAAAAGALA DTFGQHLRTF
     TLILNTLAKD KEISDRWRGF ADIADSRHLA NRVEREVVEA LVSAVRAAYP RLSHRYYALK
     ARWFGKERLA HWDRNAPLPK VPMRTIPWEQ AKSSVLEAYG AFSPTMAEIA ERFFENRWID
     APTRPGKAPG AFAHPTVPSA HPYVLVNYQG KPRDVMTLAH ELGHGVHQVL AAKNGPLMAP
     TPLTLAETAS VFGEMLTFQK LLAATKDPKR RRAMLAGKVE DMLNTVVRQI AFYTFERDIH
     TARREGELTA DRIGEIWMKV QSESLGPAIE LSAGYETFWT YIGHFVHAPF YVYAYAFGDC
     LVNALYAVYQ NAHEGFSERY LAMLAAGGTK PHAELLAPFG LDARDPGFWQ GGLGLIAKMI
     DELEAMEHSP
//
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