ID W6A8X2_9MOLU Unreviewed; 590 AA.
AC W6A8X2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN Name=pepF2 {ECO:0000313|EMBL:AHI53340.1};
GN ORFNames=SCULI_v1c10000 {ECO:0000313|EMBL:AHI53340.1};
OS Spiroplasma culicicola AES-1.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=1276246 {ECO:0000313|EMBL:AHI53340.1, ECO:0000313|Proteomes:UP000019267};
RN [1] {ECO:0000313|EMBL:AHI53340.1, ECO:0000313|Proteomes:UP000019267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AES-1 {ECO:0000313|EMBL:AHI53340.1};
RX PubMed=24534435;
RA Chang T.H., Lo W.S., Ku C., Chen L.L., Kuo C.H.;
RT "Molecular evolution of the substrate utilization strategies and putative
RT virulence factors in mosquito-associated Spiroplasma species.";
RL Genome Biol. Evol. 6:500-509(2014).
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; CP006681; AHI53340.1; -; Genomic_DNA.
DR RefSeq; WP_025363562.1; NZ_CP006681.1.
DR AlphaFoldDB; W6A8X2; -.
DR STRING; 1276246.SCULI_v1c10000; -.
DR KEGG; scq:SCULI_v1c10000; -.
DR PATRIC; fig|1276246.3.peg.996; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_021290_2_0_14; -.
DR OrthoDB; 9766487at2; -.
DR Proteomes; UP000019267; 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 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:UP000019267};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT DOMAIN 108..173
FT /note="Oligopeptidase F N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08439"
FT DOMAIN 204..569
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 590 AA; 69640 MW; F4479655ED79E271 CRC64;
MKRHQADNKY KWDFSKLYKN SQQWKDDLNL VIDKAQQISK LKNKLNNKKE FLIYLTLDKE
IDFIVAKLNQ YIHMYDIDQT NSEFQELDAL FSNAMSQVAI DLSFVTPEII KINQEQIEQY
LTDSEFESYK FMFKKIFKKS KHILENDAEE LLSKIERSRG ATAELYDTLS YADKQEHKLM
INNVEQLVDT TLFKTILEDS DAIKEQELRK QVWDIYFKNV VDRKYSYAKI YESILLKQTE
DFKVRNYTSA LEMSLFNDQV TTQIYEKLLS VAKQSIDVLK DYYLLIKDKL GLTKFFTTDR
ELKLAKEYNK KFSVDEGIAI VKESLSVLGK EYSQNLEIAM QDNMIDYYED TTKVDGAYSS
GGTGVDPIIL MNWDDKLSSL NTLAHEIGHS VHTLFSDQNQ KYPLNDYPII LAEVASTFNE
HILFDYLYSN TTNKDEKIYL LQQRIFDLVS TFYRQIQFAD FEYSAHKMVA NNEPITSENL
MKLFKDKENE YGYDIFDDKD RQVYHWPYIS HFFHSPFYVY KYAIDLVASY KLYDDFKKGN
NNIINFLKSG CYKEPLEILK DCGVDFNDNN TYTPLIKEIK RLTLELKNAC
//
