ID A0A1S8CIK4_9GAMM Unreviewed; 912 AA.
AC A0A1S8CIK4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BMI79_12300 {ECO:0000313|EMBL:OMQ22290.1};
OS Serratia oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=2034155 {ECO:0000313|EMBL:OMQ22290.1, ECO:0000313|Proteomes:UP000216021};
RN [1] {ECO:0000313|EMBL:OMQ22290.1, ECO:0000313|Proteomes:UP000216021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J11-6 {ECO:0000313|EMBL:OMQ22290.1,
RC ECO:0000313|Proteomes:UP000216021};
RA Zhang X.-X., Zhang J.;
RT "Rahnella oryzae sp. nov., isolated from rice root.";
RL Submitted (NOV-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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMQ22290.1}.
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DR EMBL; MOXD01000006; OMQ22290.1; -; Genomic_DNA.
DR RefSeq; WP_076942497.1; NZ_MOXD01000006.1.
DR AlphaFoldDB; A0A1S8CIK4; -.
DR STRING; 2034155.BMI79_12300; -.
DR OrthoDB; 9770795at2; -.
DR Proteomes; UP000216021; 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; cd06225; HAMP; 1.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR019247; Histidine_kinase_BarA_N.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF09984; sCache_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OMQ22290.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 199..251
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 298..519
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 665..781
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 814..912
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT COILED 250..288
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 714
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 853
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 912 AA; 102631 MW; 3A2FDCBAF10D4547 CRC64;
MTKYSLRARM MILILAPTLL IGLLLSTFFV VHRYNELQEQ LVDAGASIIE PLAVASEYGM
TFRSRESVRQ LVGLLHRRHS DIVRSISVFD AQNKLFVTSN YHHNYTLLQM PKDVPLPNEL
MLTRRGDSLI LRTPILSENP ILDESTGSEA HTENRLGYVA IELDLKSVRL QQYKEVFIST
LLLLLCMCIA ILFAYRLMRD VTGPIRNMVN TVDRIRRGQL DSRVEGFMLG ELHMLKNGIN
SMAMSLTAYH EEMQQNIDQA TSDLRETLEQ MEIQNVELDL AKKRAQEAAR IKSEFLANMS
HELRTPLNGV IGFTRQMLKT SLSATQTDYL QTIERSANNL LTIINDVLDF SKLEAGKLIL
EHIPFSLRET LDEVIVLLAP SAHEKGLELT LDVHNDVPEQ VIGDSLRLQQ VITNLLGNAI
KFTETGNIDI RVELRDQLER QVELEVQIHD TGIGISERQQ SQLFQAFRQA DASISRRHGG
TGLGLVITQK LVKEMNGDIC FYSQLNRGST FWFHITLDLN DGMLSPPPSL PDLRGKTLAY
IEANPTAAQA TMNMLSVTQL IVTHSPTLGK LPKNDYDYLL LGVPIPYRGS IPQHRDKLND
ALKAAKRVIL ALPSQSQVDA EEMKKLGAIG CLIKPITSNR LYPLLRMEAI QQLAAPPVRQ
RLPLTVMAVD DNPANLKLIG TLLEELVENT LLCGSGEEAI ALARENVLDM ILMDIQMPNI
DGIRAGELIR QMPHHNSTPI VAVTAHAISG EREHLLRSGM DDYLAKPIDE TMLSQVLARY
HTHEFAPEPV IPRSATELPL SLDWQLALRQ AANKEDLAHD LLQMLVEFLP EVTERVKALL
AGEVDEGILD LIHKLHGSCS YSGVPRLKQL CYYLEQQLRQ GAHSRDLEPE WLELLDEIEL
VNTEARFYLS NS
//
