(data stored in ACNUC7421 zone)

SWISSPROT: A8FPX3_SHESH

ID   A8FPX3_SHESH            Unreviewed;       346 AA.
AC   A8FPX3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   SubName: Full=Signal transduction histidine kinase, nitrogen specific, NtrB {ECO:0000313|EMBL:ABV34896.1};
GN   OrderedLocusNames=Ssed_0283 {ECO:0000313|EMBL:ABV34896.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34896.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34896.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34896.1,
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:SAAS00414205}.
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DR   EMBL; CP000821; ABV34896.1; -; Genomic_DNA.
DR   RefSeq; WP_012004422.1; NC_009831.1.
DR   ProteinModelPortal; A8FPX3; -.
DR   STRING; 425104.Ssed_0283; -.
DR   EnsemblBacteria; ABV34896; ABV34896; Ssed_0283.
DR   KEGG; sse:Ssed_0283; -.
DR   eggNOG; ENOG4105CUX; Bacteria.
DR   eggNOG; COG3852; LUCA.
DR   HOGENOM; HOG000262169; -.
DR   KO; K07708; -.
DR   OMA; NIVHNAA; -.
DR   OrthoDB; POG091H03OF; -.
DR   BioCyc; SSED425104:GH7Q-292-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
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   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
DR   PRODOM; A8FPX3.
DR   SWISS-2DPAGE; A8FPX3.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00776324};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Kinase {ECO:0000256|SAAS:SAAS00494113, ECO:0000313|EMBL:ABV34896.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00777800};
KW   Transferase {ECO:0000256|SAAS:SAAS00494184}.
FT   DOMAIN        1     35       PAS (PER-ARNT-SIM). {ECO:0000259|PROSITE:
FT                                PS50112}.
FT   DOMAIN      133    346       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
SQ   SEQUENCE   346 AA;  38459 MW;  D8616F54831A8EDA CRC64;
     MDIKHLFNNL VTAVMVIDVD LKLCYANAAA EQLLGVGSHR LTEHVLSDSF QILGVSTDLL
     SKAIRENQGL TVNTAPLVTL DNQHHTVDIT LTPLEQEQGL GLLELRQVDQ QRRIHQQLTL
     DAQQQAAQYL VRNLAHEIKN PLGGLRGAAQ LLSRELHDPQ LNEFTDLIIE QADRLRNLVD
     RLLGPQRPTQ HSLHNIHEVV QKVLNLVNMA LPPNITLKQD YDPSIPDIQM DPEQLQQAVL
     NIVQNAIQAL DTAGGEILIR TRTQHQVTIG TLRHKLVLAL SIIDNGPGIK PELLDTLFYP
     MVTGRDNGSG LGLSIAHNFA RLHGGRIDCH SKLGRTEFTI LLPIKN
//

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