ID B6IP07_RHOCS Unreviewed; 655 AA.
AC B6IP07;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF {ECO:0000313|EMBL:ACI99427.1};
GN OrderedLocusNames=RC1_2034 {ECO:0000313|EMBL:ACI99427.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACI99427.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI99427.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
CC -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU368091};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC -!- SIMILARITY: Belongs to the peptidase M3B family.
CC {ECO:0000256|RuleBase:RU368091}.
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DR EMBL; CP000613; ACI99427.1; -; Genomic_DNA.
DR RefSeq; WP_012567212.1; NC_011420.2.
DR AlphaFoldDB; B6IP07; -.
DR STRING; 414684.RC1_2034; -.
DR KEGG; rce:RC1_2034; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_5; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000001591; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09608; 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 Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 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; IPR004438; Peptidase_M3B.
DR NCBIfam; TIGR00181; pepF; 1.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 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:RU368091};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368091};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU368091};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..655
FT /note="Oligoendopeptidase F"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002844290"
FT DOMAIN 162..229
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 250..629
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 655 AA; 72355 MW; 0AF21762DC615FD5 CRC64;
MASRSPLRVR LAGAATLALL VGLTPLCLAT AQAATAVAGP GGTDAAEAPA AAPAATPDPR
YVWDLTTLFK TDADWDAERK AVLADLAGIE ALRGTLGKDA ATMRAALDRI SALSQRFERL
AVYASTQAST DSRDARNQER AGLIRQLGGR FGAAVSWLSP EVQDIGAEKV EAFIKAEKGL
APHAFRLRDI LRTKAHTLSK EAEAALAAFA PVMYAPGTTY NLLATVDIDW PTLTVEGQEV
KLNQIGYQRL REHPDRAVRK QAFDAFWTKF GQYTNTFGST LAGRVEAGTI NARLRGYKSA
VAASLADNDI PEEVYRTLVA EANKGLPTLH RYFKLRQRML DLPDLNYYDI YPSVVRIDRK
YPIAEAGTLT LAAVKPLGPE YQAKLKEALD GRWMHVYPAE GKQSGAYQTG VYGVHPFVFL
NHQDNFDGVS TFAHEWGHGM HTKLANASQP YETADYSLFV AEIASITNEI LLSDYMLSRA
ETPQERLYYL GYALEGMRGT FFRQTMFAEF ELATHDAVER GEALSGQRMT AIYCDLLKRY
HGDAEGVMKI DPAYCAEWAY IPHFYRPFYV YQYATSMAAA AYFAGQVEQK GETARDAYLS
VLRAGGSEYP YQLLKKAGLD MASPTPYQAL IKRMDTIMDE MEKILDQQAA KPARR
//
