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
//