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Database: UniProt
Entry: V4NX76_9CAUL
LinkDB: V4NX76_9CAUL
Original site: V4NX76_9CAUL 
ID   V4NX76_9CAUL            Unreviewed;       602 AA.
AC   V4NX76;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:ESQ80546.1};
GN   ORFNames=AEYBE204_04565 {ECO:0000313|EMBL:ESQ80546.1};
OS   Asticcacaulis sp. YBE204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ80546.1, ECO:0000313|Proteomes:UP000017808};
RN   [1] {ECO:0000313|EMBL:ESQ80546.1, ECO:0000313|Proteomes:UP000017808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YBE204 {ECO:0000313|EMBL:ESQ80546.1,
RC   ECO:0000313|Proteomes:UP000017808};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
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:ESQ80546.1}.
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DR   EMBL; AWGF01000002; ESQ80546.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4NX76; -.
DR   STRING; 1282363.AEYBE204_04565; -.
DR   PATRIC; fig|1282363.3.peg.902; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000017808; 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:UP000017808};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          126..193
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          212..587
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   602 AA;  66681 MW;  A6154DF16B50B823 CRC64;
     MTQITPALAI DSPDTLPIWD LTDLYSGPED PKIAADFDAA AAALKELGRL QGNFVASRGN
     PERLGLSIDQ AATLYERASD LMGGALAFTT LSSTIAREDA HVAKLEADLR NKAALISTDS
     LFLSLELNQL EDWEIEQALR ATPKAQKWRP WLRRIRASRP HELSADLEKL LLEKMPGVAQ
     WVRLFDETLT RLRAKVGKET LTLNDALTRL GSPDAKVRKA AATGLSEALK DNAPVLALAL
     NTLAFEKQVE DRWRKYPTPA ASRHLANEVD ADAVDAMADA VGESYAALSH RYYALKAKIM
     GRKSLDFWDR NAPLTTTAQK KYSWTEAKQI VLDSFAKMGP EFAARAQIFF DSPWIDAAPR
     EGKSSGAYAH PVSSSHHPYV MLNFTGERRE VLTLAHELGH AVHQTLAAPL GSILADTPLT
     LAETASIFAE GLVFEYLVAD ATPEEKKALL AGKIEDGLNS VIRQIAFHRF EEKFHALRLE
     GEVSIDQINA LWLEIMGESL GPAITLNEGY EYWWAYISHF VHAPFYVYAY AFGDLLVSAL
     MEKRRENSDA FTPLYEQLLS AGGTKTYTEA LAPFGMNPRE KAFWEMGCAR LKGLIDQFEA
     LV
//
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