ID A0A1V3A189_9GAMM Unreviewed; 1270 AA.
AC A0A1V3A189;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B1A74_02165 {ECO:0000313|EMBL:OOC11120.1};
OS Thioalkalivibrio halophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=252474 {ECO:0000313|EMBL:OOC11120.1, ECO:0000313|Proteomes:UP000189177};
RN [1] {ECO:0000313|EMBL:OOC11120.1, ECO:0000313|Proteomes:UP000189177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL17 {ECO:0000313|EMBL:OOC11120.1,
RC ECO:0000313|Proteomes:UP000189177};
RA Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA Sorokin D.Y., Muyzer G.;
RT "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL Submitted (FEB-2017) 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 -!- 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:OOC11120.1}.
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DR EMBL; MUZR01000007; OOC11120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3A189; -.
DR STRING; 252474.B1A74_02165; -.
DR Proteomes; UP000189177; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
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:OOC11120.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022519};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000189177};
KW Transferase {ECO:0000313|EMBL:OOC11120.1}.
FT DOMAIN 250..367
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 400..431
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 456..510
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 531..576
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 579..631
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 706..759
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 756..825
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 898..1116
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1147..1264
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1120..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 300
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1197
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1270 AA; 138531 MW; AF44D3558899DED2 CRC64;
METPDTVSGG RSRAAFPAFL SERLARLRDA AGELDQGECS GDCVDRLYRE VSALARVART
HGVQEILRLA ESLQATLAGL RARPNTADRE LLRLGLARLE AAAEAWARQE QGVPETRLQP
QVSADAGGGR VQVVAEVPEV GEAVAGMLRD HGFAVVLTGA EPDAAGAGGV TARVVCVGEV
TPESAVLTRL QEPGRGFLPT LVVARSWSPG ARLQAVREGA ARCLDYPLAD DTLLEQLVQI
GGVVADTGYR VLLASARPEA ADDTLVAGLR EAGLTVEVQP DPDAALAGLH GGEVEVLVLD
LDEGGCSAEE FAALLRTRDN GSSIPMLVLT ADPGRVNELM ALHPGASGVF LKPVEPRRLA
DAVVARARQQ RQVDGVTSAY RQALYERERE HLAVNEHALV SITDVAGDII YANERFARVS
GHAVSDLLGR NHRLLKSGVH TPSVYAELWE TIAAGRIWQG ELCNRARDGS LYWVETTIVP
YLDGDGLPYQ YVSIRTDITT VKRQEHRLRS SQRFANMGTW EWTPGREELQ WSERIAPLLG
HSHGDLEPTV ENFLGAVHPE DRERVENAIR SSLRRGSYLE LEHRVVWPDG TVRWLLQRGD
VERDASGGVL HMLGVSQDIT KRKQSELALT RQTTRLREAQ RLARVGHWEH DPVTGALWWS
DVVYEIFALS PGDAPVSMEG FRAFVHPEDR ERLDREYAGV LAEGRGEVFL RIRRDDGELR
HLHLIAHGES TGGREQNGRL TGTVQDVTEL QQAQEELSLF RRIFEASEQA ISVADREGRM
VYNNPAVLEM TGFEEADLAG RSYRELIPAE AEQSAREIDE IREAGGAWTG QLPIRCRNGA
VFMSSSTIGV VRDSRSEPQY IFNIFGDFTA ELQRRAELQW AREEAEQASR AKSDFLSNMS
HELRTPMNAI LGFAQLLQRD TSLGERQQSQ LDEIARAGRH LLELINEILD LARIESGRLQ
VTPEPVDVAD VVDECLSLLR PLAQEREVRL EGARAATADA PRVQADRTRL KQVLLNLLSN
AIKYNREGGR VTLLGAAGQQ GLQLEVHDTG PGLTAEQQER LFQPFDRLEA DSSGVEGSGV
GLTITRHLVE MMDGRLGVTS TPGEGSCFWF ELPLAADSDL GATPGGGPDH PAAAGASELP
ASGTPRTVLC IDDQPANLRL MEEVLGPESD LETVVAETPL KGLEEAARLA PELILLDLAM
PGMDGYQVLR ALRADDLLAG VPVLAVTADA TDPTRERALA AGFAEVITKP VDPAGLRERV
RQAFAGSAQR
//
