(data stored in ACNUC7421 zone)

SWISSPROT: A8FPK7_SHESH

ID   A8FPK7_SHESH            Unreviewed;       436 AA.
AC   A8FPK7;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   SubName: Full=Integral membrane sensor signal transduction histidine kinase {ECO:0000313|EMBL:ABV34780.1};
GN   OrderedLocusNames=Ssed_0167 {ECO:0000313|EMBL:ABV34780.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34780.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34780.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34780.1,
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:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
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DR   EMBL; CP000821; ABV34780.1; -; Genomic_DNA.
DR   RefSeq; WP_012004306.1; NC_009831.1.
DR   STRING; 425104.Ssed_0167; -.
DR   EnsemblBacteria; ABV34780; ABV34780; Ssed_0167.
DR   KEGG; sse:Ssed_0167; -.
DR   eggNOG; ENOG4105E0F; Bacteria.
DR   eggNOG; ENOG410XTWD; LUCA.
DR   HOGENOM; HOG000218774; -.
DR   KO; K07638; -.
DR   OMA; WIRPPQA; -.
DR   OrthoDB; 1031685at2; -.
DR   BioCyc; SSED425104:G1G9Y-176-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
DR   PRODOM; A8FPK7.
DR   SWISS-2DPAGE; A8FPK7.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:ABV34780.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00925724, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00926038,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00926160,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
FT   TRANSMEM     12     40       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    177       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      178    230       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      238    436       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
SQ   SEQUENCE   436 AA;  49051 MW;  4251E96E347ECB52 CRC64;
     MKWLKKFLPR SAFSQTVMLI GCLLLINQLV SYLSVATYFI QPTYQQINQL IARQVKLLFV
     DGVDIGREHL TMVDALNAKV RDDGMEIYNQ KQAREAGIDQ AVYYGFLSSQ MSEHLGGKAE
     VKIAQGDDFE IWIRPPQAPS IWIKVPLTGF NESDLSPLTL YLMVIGALSV AGGWWFARQQ
     NRPLKKLQKA AISVSMGDYP EPLPLTGSTE IVEVTNAFNQ MSHSMKQLEQ DRALLMAGIS
     HDLRTPLTRI RLASEMMVEE DEYLKDGIVH DIEDMDAIIN QFISYIRQDQ ESTREQGQLN
     DLIEDVVQAE SNREAKIEVE LNECPEIPMQ SIAIKRILSN LVENAFRYGR GWVKLSSHFD
     GKRVGFSVED DGPGIPEDQI PKLFQPFTQG DTARGSVGSG LGLAIIKRIT DRHQGEVVLT
     NRAEGGLRAQ VWLPME
//

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