ID H0G5M3_RHIML Unreviewed; 869 AA.
AC H0G5M3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SM0020_23927 {ECO:0000313|EMBL:EHK75395.1};
OS Sinorhizobium meliloti CCNWSX0020.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK75395.1, ECO:0000313|Proteomes:UP000004038};
RN [1] {ECO:0000313|EMBL:EHK75395.1, ECO:0000313|Proteomes:UP000004038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK75395.1,
RC ECO:0000313|Proteomes:UP000004038};
RX PubMed=22328762; DOI=10.1128/JB.06682-11;
RA Li Z., Ma Z., Hao X., Wei G.;
RT "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a Nitrogen-
RT Fixing Symbiont with Copper Tolerance Capability Isolated from Lead-Zinc
RT Mine Tailings.";
RL J. Bacteriol. 194:1267-1268(2012).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AGVV01000060; EHK75395.1; -; Genomic_DNA.
DR RefSeq; WP_003532998.1; NZ_AGVV01000060.1.
DR AlphaFoldDB; H0G5M3; -.
DR PATRIC; fig|1107881.3.peg.4856; -.
DR Proteomes; UP000004038; 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; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd18160; REC_CpdR_CckA-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 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; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EHK75395.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:EHK75395.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..120
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 486..709
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 751..867
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 318..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 802
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 869 AA; 94758 MW; EDBA5D638060E17D CRC64;
MTKLRQAGDY QMPVVDRGVR PGTILRIILL AIVLTASAAA FVVFKDQLEN EIVLGILGVL
AMVGIFFLVS SVIGFIEVMP QSRPDELARA FLDAHEDGTI VTDRKGRIIY ANAAYGALTG
TKSAAGIQSL ETILSRNREA TEAIYRLTNG LHEGKQGHEE FRLLKPLANG KVAGSGAHWY
RLKARVLPLE DAGSNPLYLW QIADITAERD EQERFFKELQ NAIDYLDHAP AGFFSAGRKG
EIFYINATLA DWLGIDLTKF QPGSVSIADL VAGEGLALVQ SVQAEPGLKK TKILDLDLRK
ANGQSLPVRL IHRVSSARDG APGESRTIVM SREGDDGDQS ASNAAMRFTR FFNNTPMAIA
SVDGNGRILR TNAPFMKLFA GLVSQDEVER GALIDAVVHQ SERGRLQESL AAAKDRQSDI
APIDALHPKD EGRHFRFYVN AVIDQSDQAP EEAAIIYALE ITEQKALENQ MAQTQKMNAV
GTLAGGIAHD FNNVLTAILL SADHLLLSAR PADATFADLM EIKRNANRAA VLVRQLLAFS
RKQTMRPTVL NLTDVIGDLR MLVDRMTGTN VKVEVDYGRD LWPVKTDLGQ FEQVLLNLAV
NARDAMPAGG IITLRTRNLP ASEVAALGRR ELPEEDFVMV EVSDQGTGIP PEIMDKIFEP
FFTTKDVGKG TGLGLSMVYG IVKQSGGYIY PESEIGSGTT FRILLPRHVD IPETQDEDAS
AAQSAAPARS EPVAVPMPRA EPADLTGDSA VVLLVEDEEA VRRGGKRMLE TRGYTVHEAG
SGIEALEIMD ELDGAVDIVV SDVVMPEMDG PTLLRELRKT YPDLKFIFVS GYAEDAFARN
LPADAKFGFL PKPFSLKQLA VAVREMLDS
//
