ID A0A1I1J666_9GAMM Unreviewed; 716 AA.
AC A0A1I1J666;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05660443_2635 {ECO:0000313|EMBL:SFC43966.1};
OS Marinospirillum celere.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinospirillum.
OX NCBI_TaxID=1122252 {ECO:0000313|EMBL:SFC43966.1, ECO:0000313|Proteomes:UP000199058};
RN [1] {ECO:0000313|EMBL:SFC43966.1, ECO:0000313|Proteomes:UP000199058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18438 {ECO:0000313|EMBL:SFC43966.1,
RC ECO:0000313|Proteomes:UP000199058};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOLH01000006; SFC43966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1J666; -.
DR STRING; 1122252.SAMN05660443_2635; -.
DR OrthoDB; 8573350at2; -.
DR Proteomes; UP000199058; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF33; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000199058};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 308..361
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 434..486
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 490..709
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 716 AA; 79524 MW; 59713F93FF1CF2A1 CRC64;
MKSLKILHKV SLLGLGVLVL VSFVLITGLR SNLPKEVSRL LLLEQQSDAE WLAAQAQSAL
SERQKALQYL AEVMIENDQL LPVSQLNQRL QLSVPGRQLF NGGLGVFDIN AIGIAEAPIN
SNRIGLNIAD RAHVQQVRAT LQPVITRPLV SRSLDRPSFF INVPLLDSKQ QLLGFLIGVT
ILTENNFLLD VGHDSTGMGG LFYVLDETNE LIVTASDPSQ AMQLLPEDGM NPLIDSVRRG
NVSGRARHKD GEYFIFATAS VPQMNWTIVR AVPEALVQQP MQELINKLLK ASVMLVIAGG
LILFLLLHRL LAPLKQATAN IDAMSAGQQP VELLKVKGQD EVAQLVAAFN RLFFLLDEQR
QRLSLATSSA GVGIWEYRVE TGELIWDEQM FRLYGRDAGD FSGAYSFWEQ GLHPDDLQRA
KTELQQSIDQ RRAFDTEFRV LHPDGSIHWI KANGRVQPQS EQGDTRVIGT NWDITERKQA
EIAKNQFIST VSHELRTPLT SIRGVLGLAA HGQLGVMPDT AQPMLESALR NAEHLTQLVN
DLLDMDKLES GEMHFELVEL DLLALLRESI DRNQSFADQH QVTLRLQPDA VCTPVLADPQ
RLHQVMSNLL SNAIKFSLPG SRVEIHFERF AEHVRVSVTD QGQGVPEAFR DRIFQRFAQA
DASDTRQKGG TGLGLAITRA VIEKMQGEIG YESSPGQGSV FYFTISAARN HPHKAF
//