(data stored in ACNUC7421 zone)

SWISSPROT: Q3KK74_PSEPF

ID   Q3KK74_PSEPF            Unreviewed;       680 AA.
AC   Q3KK74;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   SubName: Full=Putative oligopeptidase A {ECO:0000313|EMBL:ABA71832.1};
GN   OrderedLocusNames=Pfl01_0088 {ECO:0000313|EMBL:ABA71832.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA71832.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA71832.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA71832.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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}.
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DR   EMBL; CP000094; ABA71832.1; -; Genomic_DNA.
DR   RefSeq; WP_011331810.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0088; -.
DR   EnsemblBacteria; ABA71832; ABA71832; Pfl01_0088.
DR   KEGG; pfo:Pfl01_0088; -.
DR   eggNOG; COG0339; LUCA.
DR   HOGENOM; HOG000245986; -.
DR   KO; K01414; -.
DR   OMA; VENTAWQ; -.
DR   BioCyc; PFLU205922:G1G4S-88-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   Gene3D; 1.10.1370.10; -; 1.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KK74.
DR   SWISS-2DPAGE; Q3KK74.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN      226    665       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   680 AA;  76838 MW;  680A4108229D3466 CRC64;
     MPDTNPLLQH WTLPPWPAIH AEHLLPAVNS IIADNRRIIA QVIASQTEHP GWDDLVLSID
     EADARLGEVR SILETLSMVR SDDPVWLVES AKAHLAINQY RSEKAHNRRL YETYQRLAQS
     SIAGSFDEAR NIALSRILRR FKQSGIELPT EQQQELARLN REIGGLEFVF LDNLERWAEA
     WSKRVDDVAL LTGLPPAMKD RLALAARQTG HDGWLIRLDQ NTFQHILKYA ENRALREECY
     VAYMTRASDR GPLAGRFDNA PVLKKLLALR QQKARLLGHE NAAQLSLAKN SAGTTAWVSG
     FLQRQAAQLA PTLAQDAEQL TDFAQQRGID RVQPWDEDFL AEQWRQQQFP GALENLRDYF
     PLEGTLRRLL LFCERMFGIR IVEQSGGGHL HDDVRLLEIS EDEQVIGYIY LDPFHRDGAA
     DFPGTFTLRN RRINAEGRPA LPIALLYSNF TPASDTHPCR LELHDLRVLF HEFGHCLQHV
     LTRSPHHSLS GILQLGHEAA EFSGQLFEQW CLSREFLLWL GAHFQTGKRL SAARVDAALS
     ASQAHSARQQ AFLLMGAMID FELHLTHGDG RSVEETCTDV QRSLGHLQLP DDHRFANGFD
     YMVTQYDASV YAYVWSGVLA QEAFKRFSQD WVFNAQTGRE FRATFFAPGA GRPLLDAVEA
     FIGRPVAGLV DGEAGRVTSD
//

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