(data stored in SCRATCH zone)

SWISSPROT: A8FPY0_SHESH

ID   A8FPY0_SHESH            Unreviewed;       931 AA.
AC   A8FPY0;
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=Histidine kinase {ECO:0000313|EMBL:ABV34903.1};
DE            EC=2.7.13.3 {ECO:0000313|EMBL:ABV34903.1};
GN   OrderedLocusNames=Ssed_0290 {ECO:0000313|EMBL:ABV34903.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34903.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34903.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34903.1,
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; ABV34903.1; -; Genomic_DNA.
DR   RefSeq; WP_012004429.1; NC_009831.1.
DR   ProteinModelPortal; A8FPY0; -.
DR   STRING; 425104.Ssed_0290; -.
DR   EnsemblBacteria; ABV34903; ABV34903; Ssed_0290.
DR   KEGG; sse:Ssed_0290; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000223373; -.
DR   OMA; NDVSERI; -.
DR   OrthoDB; POG091H02OU; -.
DR   BioCyc; SSED425104:GH7Q-299-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:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 2.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; A8FPY0.
DR   SWISS-2DPAGE; A8FPY0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Kinase {ECO:0000313|EMBL:ABV34903.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:ABV34903.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     12     34       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    180    198       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      414    633       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      798    920       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   MOD_RES     850    850       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   931 AA;  104409 MW;  0FA75D6F804546DE CRC64;
     MAPSSYRHSI GFRLNLSTLI IGFIICVILS GYFIQETRER LKVQAHHELT QITDSLKLAL
     ETNSQTSNMI RVVGVLSTYP NITRLTVIKA SDLSISADSL VQNNGKRANL VFSNTIMKLI
     NNPAKSSQRD QGILIDNSLH QSVKIHLVDP QANRLKPYII YLEYNKQALE RILQQARNHL
     MLIVIGGLIL LLLINIFIQR VVVLKPLSKM TQQLLNQDNS EQIPEPLQVS TNDEFSILAN
     SYNGSIHKQL LQKAEVEKSH RYIKNMASAL PVHLLYVDID KKIQFINQYS LQWLAKPMEE
     VLTQTCRQVL PSQLFSLIER PIETALQGDS ITLDAEFFHK NMSLFFHITH IPDIDNEGRI
     KGIFICIEDR TQTRDNEKKI EKYAHQLEMN NLALDDARET AEAAAQSKSE FLACMSHEIR
     TPMNGVLGML TLLERTALDQ SQRNHLDTAQ GSARNLLGLI NDILDFSKIE SGKFPIESVN
     FSLTNLLNET IRPLAIRAQE KGIELVSDIT DITSQSFKGD PTRISQVLTN LIGNAIKFTE
     KGSITVYVKQ NDDIEPRLNF SVEDTGIGLA SNQLEKLFQP FTQADSSTTR HFGGTGLGLS
     IAKRLTELMG GSISVVSTEG KGSKFSFNVR VEIASKDDLY ATDLNSLPIL FFSRGTRADQ
     VLGKTLNLLN ASLKVVKAAR LANFKPASIS DTYRPKLTII HLPAGQEAIE TELAKLASNT
     DLPDTPILLF IAAIDESIMT QYLNEQIFTY LCNPLHLEQL LIALKQIDQT APHLVQRLAP
     QTQRDWDLKS YFEDRLPKLL LVEDNKTNQM VAQGIIAEFG LEIDIASDGE QAIEILKDSI
     TSPYQLIFMD CQMPRLDGYQ TTQMIRAGYT GHQYKHIPII AMTANAMVGD RERCLQAGMN
     DYISKPLDPD DIKQALLSTL AGHDTESEMR N
//

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