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
//