ID A0A1F8LUS9_9CHLR Unreviewed; 602 AA.
AC A0A1F8LUS9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN ORFNames=A2Z74_01795 {ECO:0000313|EMBL:OGN90124.1};
OS Chloroflexi bacterium RBG_13_46_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797619 {ECO:0000313|EMBL:OGN90124.1, ECO:0000313|Proteomes:UP000180311};
RN [1] {ECO:0000313|EMBL:OGN90124.1, ECO:0000313|Proteomes:UP000180311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGN90124.1}.
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DR EMBL; MGMM01000010; OGN90124.1; -; Genomic_DNA.
DR Proteomes; UP000180311; Unassembled WGS sequence.
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 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:SF77; 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: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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 117..185
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 207..587
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 602 AA; 68326 MW; 68E30DC2763E2126 CRC64;
MVGLTVPKRN EIKAENSWNA PSVFPSMQSW ETEFRDVEAS LPLLDSSKEK LAEGAVSLFS
SLQTIENIQR RTMKLMVYAS MSYSVDTQDQ VSIGMYDRXX XLVGKMQGAT AFLNPALLAL
GNEKLKRWMT EDPRLTVYSH FIDNLFRKNA YVRSNEVEEL MGMLASPFSG PDSIYSSLTD
ADFKFKPAIA GDRREIPVTQ STIEAVLHDP DREVRRTGWE NYSDTFLGFK NSLANTLLSS
VKQDVFEMQV RRHKSTLEAS LFEDNIPVEV FNNLISIFKK NLPTWHKYWR LRRKWLGVDV
LHPYDIWAPL TTSKPRLDYR QAVEMIAAGM RPMGDEYVQI LRQGCLVDRW VDVYPNQGKT
AGAFSSGSYD THPFICMSFT DDVNSLSALA HELGHSMHSY LTRRHQPFVY GDYSLFIAEV
ASNFHQAMVR AHLLKTNTDP LFQIALIEEA MSNFHRYFFI MPTLARFELE VHQRVERGEG
LTANTMIGLM TDLFIEGYGG EMHIDHDRVG ITWATFGHLY YNYYVFEYAT GISAAHALSN
RILTGVPNAV QDYLSFLSAG GSVYPLDALK IAGVDLSKPY SVEETFGVLS GYVDKLETLL
PV
//
