ID G4E7Y8_9GAMM Unreviewed; 818 AA.
AC G4E7Y8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ThisiDRAFT_2417 {ECO:0000313|EMBL:EGZ43526.1};
OS Thiorhodospira sibirica ATCC 700588.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thiorhodospira.
OX NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ43526.1};
RN [1] {ECO:0000313|EMBL:EGZ43526.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ43526.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL Submitted (SEP-2011) 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:EGZ43526.1}.
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DR EMBL; AGFD01000061; EGZ43526.1; -; Genomic_DNA.
DR RefSeq; WP_006788445.1; NZ_MU255056.1.
DR AlphaFoldDB; G4E7Y8; -.
DR STRING; 765914.ThisiDRAFT_2417; -.
DR PATRIC; fig|765914.3.peg.2395; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 5563233at2; -.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_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 NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:EGZ43526.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EGZ43526.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 12..62
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 80..302
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 321..443
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 471..587
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 639..739
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 375
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 520
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 680
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 818 AA; 88569 MW; 3497AA5E50D1CF62 CRC64;
MLAQLEGDGE VRNFEVEMRL PDGSERVMLA NFVRLDYQGE PGILGWLLDI SERKQAELAL
AHACDAAEEA TRAKSDFLAN MSHEIRTPMN AILGMSHLAL QTDLTPKQRN YIDKVHRSAE
ALLGIINDIL DFSKIEAGKL DMESAEFRLE DVLDNLANLV GLKAEEKGLE LLFDTHQALP
TALIGDALRL GQVLINLGNN AVKFTEPGGE VLVRVTVFEE SPHFVTLHFA VRDSGIGLSP
EQQQRLFQSF TQADSSTTRR YGGSGLGLAI CKRLTALMDG QIWVESALGA GSTFHFTARF
GKQTGLPSAR RQRPEALPAL RILVVDDNQS AREVLGAMLT AFGFYLEEAA SGAQAIARLA
QAEQDGTPFE LVLMDWKMPG MDGLATTRTI QHDHLLLKAP TVIMVTAYGR DEAQRAADGL
QVAGFLTKPV VPSTLLDAIL TALGHQAVTH HRRSERQDST AEAVAQLRGA RILLVEDNAI
NQELALELLT SNGIRVAVAN NGQEALELLA EQTFDGVLMD CQMPVMDGYT ATRAIRQNPA
WGDLPVLAMT ANVMTGDRER AIAAGMNDHI GKPVKVREML ATMACWIAVK EKATTHEHPS
IPRKEEEQDK ALLSTGVESW LSALPGIDTQ TGLSIAQGHQ ALYRRLLMRF CDSQAHFADD
FAAALASLEQ DPEAATRCAH TLKGVAANIG AEGVREAAAA LEAACRDGAD SKLIETHLQA
TLAALKPVLN GLAQLDQLAT AEPEATPSNT LDPEAITRAL QRLRELLSDD DTEASVFIAD
LSRQLGTHPL AVALRPVAKA VATYNFEAAL EALDQMSS
//
