(data stored in ACNUC7421 zone)

SWISSPROT: A8FPH9_SHESH

ID   A8FPH9_SHESH            Unreviewed;      1064 AA.
AC   A8FPH9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 80.
DE   RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00703354};
DE            EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00703354};
GN   OrderedLocusNames=Ssed_0139 {ECO:0000313|EMBL:ABV34752.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34752.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34752.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34752.1,
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.
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine. {ECO:0000256|SAAS:SAAS00703347}.
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DR   EMBL; CP000821; ABV34752.1; -; Genomic_DNA.
DR   RefSeq; WP_012004278.1; NC_009831.1.
DR   ProteinModelPortal; A8FPH9; -.
DR   STRING; 425104.Ssed_0139; -.
DR   EnsemblBacteria; ABV34752; ABV34752; Ssed_0139.
DR   KEGG; sse:Ssed_0139; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   OMA; DVISSAC; -.
DR   OrthoDB; POG091H03T5; -.
DR   BioCyc; SSED425104:GH7Q-142-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47226; SSF47226; 2.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; A8FPH9.
DR   SWISS-2DPAGE; A8FPH9.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00776284};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Kinase {ECO:0000256|SAAS:SAAS00577625, ECO:0000313|EMBL:ABV34752.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00776426};
KW   Transferase {ECO:0000256|SAAS:SAAS00577260,
KW   ECO:0000313|EMBL:ABV34752.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00577723}.
FT   TRANSMEM     20     40       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    325    346       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      347    400       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      425    650       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      810    928       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      959   1062       HPt. {ECO:0000259|PROSITE:PS50894}.
FT   MOD_RES     859    859       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   MOD_RES    1000   1000       Phosphohistidine. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00110}.
SQ   SEQUENCE   1064 AA;  119381 MW;  2AD2CCF03018681C CRC64;
     MPFRLLTQWL SLTSIGSKVI LSMAGISLLV LMLSASNFIM NTRVKEDTTE VSTHEIPKAI
     AAINMLDEIG DMNSNILEYV LGEVDERDDF DQNQITFLQY LATLKSALKA HDRRIDEIEE
     LFNDFHTSAR ANVFNRYNPN NEAWAKQRVD GLTNVTGHKL EVLLDSLKES EIKDVGSQPD
     LNEVIHDDLP GVRYYLELVD EAGDMTANLT EYISGIYEAK NAFIENAQDF EEYLTKLQPL
     EQKPEEIALL AEVEALYKVL RDGGFEVFQR YNSSNKLEAI TAIDELEHQT FARLERLLDD
     VSIDAERNTN LELLGLRQMT ISNQYVLIVS LFLVLSLCIS IIYFSYRIIT RPITKLSSTM
     KQLADGDTEV DVVYRDRQDE VGNMAQAVEV FKTNMIARNA AEQELVMAKD NAEAASKAKA
     SFLATMSHEI RTPMNGIIGM IDLLLTSSLN RDQRSMTNTI RDSSFSLLNI INDILDFSKI
     EAGKLELESL NFSISELLES VIDTITPNAD EKRVTLELYT DPNIPHHIQG DPVRIRQVLF
     NLVGNAVKFS AVQDSRGEVR ITLKKKELSN QLVFLTIEIQ DNGIGIEAKQ LERLFQPFTQ
     AESSTTRQFG GTGLGLAICQ NLVNLMGGKI DVSSTVGKGS IFKVNLSFPY IERPSPLTHD
     YPKVIVIDDI HSEPLSVRVK EYLSSREVNL VSMPYMNTSD HLRDNVETWA QVVIATDQLE
     QSRQQVEQNL TDAERKNIRF LVLKPTSRGD GIIDDNTFSI AASPLKISTL FYGLHVALGR
     ESPLDSSAHE ADTLSHTPLS ITDAEKAGRL ILVAEDNQTN QEVIKRQLSK LGYSCIVADD
     GVHAEELYPT YKFAMVLTDC HMPRRDGYEL TRVLRSMQKK SGIKVPIIAI TANALVGESE
     KCIAAGMDDY LSKPVELVKL NKMLKKWLSS SFKNSNDADK EQTDTERRYL DQGVISLVFA
     DDREDYIAAL SDFMEIILPQ MKSMVKERNF NISAIGELAH KLKSSAKTIG LLSIGDHCET
     IEAIAKEPDN QQARVSITER LDSIEDLLPQ IEKEITDVIS SACR
//

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