ID A8FPK7_SHESH Unreviewed; 436 AA.
AC A8FPK7;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE Flags: Precursor;
GN OrderedLocusNames=Ssed_0167 {ECO:0000313|EMBL:ABV34780.1};
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; 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., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA 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; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000821; ABV34780.1; -; Genomic_DNA.
DR RefSeq; WP_012004306.1; NC_009831.1.
DR AlphaFoldDB; A8FPK7; -.
DR STRING; 425104.Ssed_0167; -.
DR KEGG; sse:Ssed_0167; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_27_6; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000002015; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd16950; HATPase_EnvZ-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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 PANTHER; PTHR44936:SF5; SENSOR HISTIDINE KINASE ENVZ; 1.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABV34780.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 178..230
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 238..436
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE: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
//
