(data stored in ACNUC7421 zone)

SWISSPROT: A8FPM6_SHESH

ID   A8FPM6_SHESH            Unreviewed;       688 AA.
AC   A8FPM6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 74.
DE   SubName: Full=CheA signal transduction histidine kinase {ECO:0000313|EMBL:ABV34799.1};
GN   OrderedLocusNames=Ssed_0186 {ECO:0000313|EMBL:ABV34799.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34799.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34799.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34799.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000821; ABV34799.1; -; Genomic_DNA.
DR   RefSeq; WP_012004325.1; NC_009831.1.
DR   ProteinModelPortal; A8FPM6; -.
DR   STRING; 425104.Ssed_0186; -.
DR   EnsemblBacteria; ABV34799; ABV34799; Ssed_0186.
DR   KEGG; sse:Ssed_0186; -.
DR   eggNOG; ENOG4105CBS; Bacteria.
DR   eggNOG; COG0643; LUCA.
DR   HOGENOM; HOG000255263; -.
DR   KO; K03407; -.
DR   OMA; VDVGAMM; -.
DR   OrthoDB; POG091H05CG; -.
DR   BioCyc; SSED425104:GH7Q-189-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   Gene3D; 1.10.287.560; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR002545; CheW.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF50341; SSF50341; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
DR   PRODOM; A8FPM6.
DR   SWISS-2DPAGE; A8FPM6.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00776324};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Kinase {ECO:0000313|EMBL:ABV34799.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00777800};
KW   Transferase {ECO:0000313|EMBL:ABV34799.1}.
FT   DOMAIN        1    105       HPt. {ECO:0000259|PROSITE:PS50894}.
FT   DOMAIN      340    543       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      545    680       CheW-like. {ECO:0000259|PROSITE:PS50851}.
FT   MOD_RES      48     48       Phosphohistidine. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00110}.
SQ   SEQUENCE   688 AA;  76410 MW;  78F65EA1975D4EE4 CRC64;
     MEIDLSQFSQ VFFEESLEGL ESMESELLKL DVNEPEDESI NTIFRAAHSI KGGSATFGFS
     QVANYTHLLE TLLDEIRDGR RQMTSEHQDM LLLSVDLLRN MIDALMRKTD FDDPLLSQLE
     KRFTSELEGA AEDIQDEDAT QADAEQAPDE QLWHIDFQAG IDILRCGNDP LLMFTELRQL
     GELTVKLAEI NHPDFGDIDP EACYLSWHLE LITDQKIERL KEVFEWVEDE CTIHYSSSVI
     DTGETRELQG TSESPQASPV PESTQASTST SDSLPAEVVK PKIVSQAKSP EGGSIRVSIE
     KIDLLINMVG ELVITQAMLG QIGQQDEIDE ESLLSMKQGL EQLASHTRDL QESVMQIRML
     PISFAFNRFP RLVRDIGQQL GKKVDLILNG EDTELDKTVM EKIVDPMVHL VRNSLDHGLE
     TPEIRVSKGK PETGSITLNA FHQGGNIIIE IIDDGAGLDT DRILQKARDK GLVAEDEELS
     TEAIHQLIFK AGFSTADAVS DLSGRGVGMD VVRRNINELN GTIELKSTQD KGSRFTIRLP
     LTLAILDGQL VRIGHHTYVV PLVSIHESLQ VEPQRINRIS ENHELVRLRD EYLPVIKVFQ
     EFDHEADAIE IKDGLVMVVD SNNEKVGLLV DELLSQQQVV IKSLEDNYSK VPGVSGATIL
     GDGTVALIID ISGLVSLAGI TNTNEHAA
//

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