(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZL01_PSEAB

ID   A0A0H2ZL01_PSEAB        Unreviewed;       465 AA.
AC   A0A0H2ZL01;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 9.
DE   SubName: Full=Putative zinc protease {ECO:0000313|EMBL:ABJ15338.1};
GN   OrderedLocusNames=PA14_04890 {ECO:0000313|EMBL:ABJ15338.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15338.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15338.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15338.1,
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).
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DR   EMBL; CP000438; ABJ15338.1; -; Genomic_DNA.
DR   RefSeq; WP_003084498.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZL01; -.
DR   EnsemblBacteria; ABJ15338; ABJ15338; PA14_04890.
DR   KEGG; pau:PA14_04890; -.
DR   KO; K07263; -.
DR   OMA; EDTGSRM; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
PE   4: Predicted;
DR   PRODOM; A0A0H2ZL01.
DR   SWISS-2DPAGE; A0A0H2ZL01.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Hydrolase {ECO:0000313|EMBL:ABJ15338.1};
KW   Protease {ECO:0000313|EMBL:ABJ15338.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     33       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        34    465       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002603498.
FT   DOMAIN       50    188       Peptidase_M16. {ECO:0000259|Pfam:
FT                                PF00675}.
FT   DOMAIN      204    387       Peptidase_M16_C. {ECO:0000259|Pfam:
FT                                PF05193}.
SQ   SEQUENCE   465 AA;  51947 MW;  4CEBE48712EB5F17 CRC64;
     MAARKVQITM KTPARRRVGL LLASLCLPLF AQAAETQPTH EFSLDNGLKV IVREDHRAPV
     VVSQLWYRIG SSYETPGLTG LSHALEHMMF KGSRKLGPGE ASRVLRDLGA EENAFTTDDY
     TAYYQVLARD RLPVALEMEA DRMAHLSLPA DQFKSEIEVI KEERRLRTDD NPNALAFERF
     KAAAYPASGY HTPTIGWMAD LQRMTIDDLR HWYESWYAPN NATLVVVGDV TADEVKTLAK
     RYFGEIPWRQ LPPARKPLEL AEPGERRLKL YVRTQLPNLI MGFNVPSLGS SENPREVNAL
     RLIGALLDGG YSARLASRLE RGEELVAGAS TYYDAFNRGD SLFVLSATPN VQKGKTLEQV
     EAGLWKQLDD LKQNPPSAAE IERVRAQMIA GMVYEKDSIA AQASSIGQLE SVGLSWKLID
     QDLEALKAVT PDDIQKAART YFTPSRLTLA QVLPVKAEEK EARHE
//

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