ID A0A1V3A153_9GAMM Unreviewed; 1452 AA.
AC A0A1V3A153;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B1A74_02660 {ECO:0000313|EMBL:OOC11046.1};
OS Thioalkalivibrio halophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=252474 {ECO:0000313|EMBL:OOC11046.1, ECO:0000313|Proteomes:UP000189177};
RN [1] {ECO:0000313|EMBL:OOC11046.1, ECO:0000313|Proteomes:UP000189177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL17 {ECO:0000313|EMBL:OOC11046.1,
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 -!- 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:OOC11046.1}.
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DR EMBL; MUZR01000007; OOC11046.1; -; Genomic_DNA.
DR STRING; 252474.B1A74_02660; -.
DR Proteomes; UP000189177; Unassembled WGS sequence.
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; 2.
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; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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; IPR013655; PAS_fold_3.
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; 2.
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; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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; SSF51905; FAD/NAD(P)-binding domain; 1.
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); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000189177};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 434..490
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 508..560
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 561..633
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 636..688
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 706..927
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 951..1072
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1100..1216
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1266..1361
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT REGION 1076..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1005
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1149
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1305
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1452 AA; 159156 MW; 38893E119EBB75C4 CRC64;
MLLAERSRAV APALRDWAGI RMFTSWQQCT SPLGRDALRG QGHALPDPDA FPTAGEFRRE
YCERLAGVLA HRDCDLLLET RVLAASRDGM RANTGIGDPE RARHPFRVLV DEQGRERQLE
ADLLIDTTGV AGHPQWLGPG GLPASGEREL GGRILYGPRA PEGEEGQALP PAECILVAGG
GAEAALAVEY WLDPPTGSPP VELLWAFEEP VPLPPDWPQR DPFPERGARF ARVLEATAGD
RGARRLPQTQ VVRLEHGPGV RGGLDVELRG PDGTRRMSVD RVHALTGHVP DNAWLETLQF
HACYATGAPM GLAAAMLATV EDSHELWHSL GVSTVGNPEP GLFVLGRKSY GRSPGFVLPV
GLGQIVETFQ SITGDTSLDL YGDTVPRQGN RPGGAAIESA QPVTCDLPPA ATDTAGPAGR
DAVIPGDGGE DAAADYHFRV IAENLKEVVF QTDLEHRITY LSPSWSEVTG LAREPFIGHS
WMDLLHPEDQ GYGRNQCDAF VGDRLAEYNE ELRVRTSEGA VRWMDVTARV LRDRQGRARG
TVGSMLDVTR RRESEAELRE SQERFRLISD LATDWIYWLT PEFEFRYCSP SCQAVTGYGD
AEFYRNPDLL REIVHVEDRE GFDQHLYEIH EKHVDGAFDF RIVTRAGEER WLRHHCTPVY
AESGLYMGQR AANYDITDRI RAEEALTRAR DEAESATRAK SEFLANMSHE IRTPMNAIIG
MTHLARRTEL TPKQRGYLDR IDSASQALLG LINDILDFSK IEAGKLELEE SPFALEDVLR
NVWDIVGLKA EDKGLELVHR VDPALPHHLT GDALRLGQIL TNLVGNAVKF TEEGEVVVGA
TCERMEEDEA VLRFEVRDTG PGMSREETRR LFQSFTQLDG SVTRQQEGTG LGLAISRQLV
EMMGGEIGVE SEPGRGSTFH FSVRLGLNTA AGDPHETLGE RLTGAELAGR RALVVDDNAS
ARETLEEMCR YLGMEVEVVP SGAAALAQID QALEEGRPYD LVLTDWRMPG VDGIEVAQRI
KAHEGARMPA VLMVTGFARE EVLGRAERAG VDGILLKPVS QSTLLDTLSG LFHVHPEETS
PMPAPAEKGK RESADMSGSR VLLVEDNVIN RELATELLQD LSCEVTWAED GREGVEKARN
ETFDLILMDI QMPRMDGLTA TRRIRARPDL AEIPIIAMTA HAMEGDRERS LEAGMDDHVT
KPIDPQVLEE TLGRWMNNVP GAGDSQACEA GADAMQAAPE PAPEPDLPES LPPFDLPAAL
ARCGGKPALL RKMLAGLERD YSDAGRRLRE WLEQDRTEDA QRLAHSLKGV AAALEAAELR
TAAEAVELAL RDGDPETQEL ETRLQSLEAA LAEATAAVAG LGRAARGGGD RENRSRASAG
PRGPFPHEAL RALRERVAQN QLGARREFDG LRPQLEGRGL DPEVQAIAEG LESLDFDAAL
TALDRLLDGM RE
//
