(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZK71_PSEAB

ID   A0A0H2ZK71_PSEAB        Unreviewed;       681 AA.
AC   A0A0H2ZK71;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   SubName: Full=Oligopeptidase A {ECO:0000313|EMBL:ABJ15024.1};
GN   Name=prlC {ECO:0000313|EMBL:ABJ15024.1};
GN   OrderedLocusNames=PA14_00790 {ECO:0000313|EMBL:ABJ15024.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15024.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15024.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15024.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15024.1; -; Genomic_DNA.
DR   RefSeq; WP_003136955.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZK71; -.
DR   EnsemblBacteria; ABJ15024; ABJ15024; PA14_00790.
DR   KEGG; pau:PA14_00790; -.
DR   KO; K01414; -.
DR   OMA; INGVAWD; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.20.1050.40; -; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR001567; Pept_M3A_M3B.
DR   Pfam; PF01432; Peptidase_M3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZK71.
DR   SWISS-2DPAGE; A0A0H2ZK71.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
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      224    675       Peptidase_M3. {ECO:0000259|Pfam:PF01432}.
SQ   SEQUENCE   681 AA;  76065 MW;  1B337FC67B4F165D CRC64;
     MSANPLLQAY DLPPFSSIRP EHVKPAIERI LADNRAAIAR LLETQREQPT WKGLVLAMDE
     LNDRLGAAWS PVSHLNAVCN SAELREAYEA CLPELSAYST ELGQNRALFE AYEALAKSPE
     AAGFDVAQKT ILEHALRDFR LSGIDLPADK QKRYAEVQSR LSELGSRFSN QLLDATQAWT
     KHVTDEAALA GLTDSAKAQM KQAAEAKGLD GWLISLEFPS YYAVMTYADD RALREEVYAA
     YCTRASDQGP NAGQNDNGPV MEEILDLRQE LAGLLGFANY AELSLATKMA ESSDQVLSFL
     RDLAVRSKPF AARDLEQLRA YAAEQGCTEL QSWDAGYYAE KLREARYSVS QEALRAYFPV
     DKVLSGLFAI VERLYGIQIR ELHDFERWHA DVRLFEILEN GEHVGRFYFD LYARANKRGG
     AWMDGARDRR RDAQGRLIDP VAYLVCNFTP AVNGKPALLT HDEVTTLFHE FGHGLHHLLT
     RVEHAAASGI NGVAWDAVEL PSQFMENWCW EPEGLALISA QYETGEALPQ DLLEKMLAAK
     NFQSGMMMVR QLEFSLFDFE LHATHGDGRS VLQVLEGIRD EVAVMRPPAY NRFANSFAHI
     FAGGYAAGYY SYKWAEVLSA DAFSRFEEEG VFNPDTGRAF REAILARGGS REPMLLFVDF
     RGREPSIDAL LRHSGLVGEA A
//

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