ID I0HTD5_RUBGI Unreviewed; 1043 AA.
AC I0HTD5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=RGE_29330 {ECO:0000313|EMBL:BAL96272.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL96272.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL96272.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(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};
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DR EMBL; AP012320; BAL96272.1; -; Genomic_DNA.
DR RefSeq; WP_014429133.1; NC_017075.1.
DR AlphaFoldDB; I0HTD5; -.
DR STRING; 983917.RGE_29330; -.
DR KEGG; rge:RGE_29330; -.
DR PATRIC; fig|983917.3.peg.2861; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_4; -.
DR Proteomes; UP000007883; Chromosome.
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; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 5.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; PTHR45339:SF3; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
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; 4.
DR SMART; SM00091; PAS; 5.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAL96272.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW Transferase {ECO:0000313|EMBL:BAL96272.1}.
FT DOMAIN 28..93
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 96..147
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 222..274
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 418..488
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 491..543
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 673..893
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 920..1038
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 971
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1043 AA; 115188 MW; 8EAE58938C3F79E6 CRC64;
MARHPVTEAD DPAAGPLADD IPSLATTLLA SISDGVNVID GRRRIVYTNR AFDEMFGYAP
DELLGQDAAV LNADGQRSGE LLAQEIVHTL EASGAWTGEL LNRRRDGSRF WTHASVTSWR
DPQRGTLWVT VQRDITAMRE AQAQRRIAEQ RFQLAQDAGH IGIWDFDLAS GSVYWSPESL
RLCGLPDDEP NLSYEDWRAR IHPDDLALID AGWAQVWRGE SFNVEYRMRH GRDGWRWLYS
AGRPVIDDEG RLMRVLGINL DITERRRAAA ELEAHRDHLA DLVAQRTQCL EEQTRFLQTM
SDALPALVGY WDTALHNGFA NRAYREHFGL STERIRGTTM RELLGDELFA ANQASAAAAL
AGTPQRFERS IRRPSDGRAM HVWVQYIPDV CDGRVVGFFV LATDVTALHE ANEQLRRQAA
ELDDLYHHAP CGYHSITPEG TVRKINDTEL AWLGYRREDV VGRHITEFMT PESVRTVHET
MPRFFAQGRI ESLELELVRR DGRRLPVLLS ATAVRGDDGR PVLSRSVLVD YSQLREQQRV
LRQVLSAAPV AVRIARARDR AVLFANDAFY ALLDRPRAQA DRIDIRAHYC DPAVFDEIGA
QVAAGEAVLN RLVELHRPGQ PETPHVWALS SYMPIVYENQ PAVLAWLFDV SELQRARDDA
EEAMRAKSSF LANMSHEIRT PLNGIVGMAH LVGRGPLEAV QRAQLAKLVA ASEHLKSIIN
HVLDIAKIDA GKLTLCTAPL RLEAVAANAL AMLEGEARAK GLQLLLELQP PLPAVLGDAT
RLEECLLNYV YNAVKFTERG SVTLRVRTDG EDERGVLVRF EVRDTGIGIK AGTMRKLFAE
FEQGDAAGAH QAHGTGLGLA ITRRLARLMG GDTGAASQPG QGSLFWFTAR LPRAPAAGSE
AAATAEDAEA ELLARHRGRR VLLAEDNDIN VDVARSLLEE VGLQVEVAAN GAEAVACVAA
RGADYGLVLM DLQMPVMDGI AATRAIRASG EHASLPIVAM TANAFDEDRA ACLAAGMDDF
LAKPVVPEEL FATVARWLSR PRH
//
