ID G9ZTZ6_9PROT Unreviewed; 840 AA.
AC G9ZTZ6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF9946_00009 {ECO:0000313|EMBL:EHM03526.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM03526.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHM03526.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:EHM03526.1}.
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DR EMBL; AGEZ01000001; EHM03526.1; -; Genomic_DNA.
DR AlphaFoldDB; G9ZTZ6; -.
DR STRING; 1054213.HMPREF9946_00009; -.
DR PATRIC; fig|1054213.3.peg.10; -.
DR eggNOG; COG0642; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_21_5; -.
DR OrthoDB; 9801651at2; -.
DR BioCyc; ABAC1054213:G1H32-9-MONOMER; -.
DR Proteomes; UP000003292; 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; cd12914; PDC1_DGC_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF00072; Response_reg; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EHM03526.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW Transferase {ECO:0000313|EMBL:EHM03526.1}.
FT DOMAIN 334..559
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 574..695
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 718..835
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 767
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 840 AA; 88387 MW; 76F6C262E693D886 CRC64;
MGLVGLCLAG FYGLLLDRAQ RDAMEDARRL TSGVVAAVSD QLSHSLETIG GLLTDTASRL
SAESALPLAQ QLHGRIRDVA QLRAVLLLDA NGQVVASTES SLRGLSLADR AWFQSQRLGA
QTPRLGSPEP GQYPLTRNLI GSTSQQVAAA GNWSVPYALP LRGADGGFRG SVVALLNAEY
LSTVARRNAE AFQVNLRLYN GAGLLLAGSM PGTAGIGELR AAAWPFHGTA ARPGSAHWVG
PDEAGTLVVA ALATSGPDGF TVEAATPVDA ALSSAHHLGG ILLVGVSAVG GVTLMALWLL
FRQASDLKRQ GEALSASEAS AHAATRAKEE FLASMSHEIR TPMNGIIGMT GLLLDTRLMT
LQRHYAETIG RSAEHLLMVL NDILDFSKLE AGMVEPEHVP FDIEQEVATI AELFGPRGDD
NSVELVCDLD PELPRMVLGD PGRFRQILFN LAGNAVKFTS EGWIEISVSL LPVEGERAKD
RARLVCSVAD TGIGIDPDKI PLLFERFTQA DASISRRYGG TGLGLAICRR LAEQMGGGVG
AEPREGGGSV FYFDILVGLP EPVTLRPSRL AGRRILLAEA LPAARRCMAQ HVRAAGGQAE
EADNARDALA LLREAARQGQ AYAAAVLGGL GATGQEGLAL AYAIRAEPSL EQTPLILCGS
GATLANVPAS TMPAERVLLK PVIPGRLRDA LEWLLLPELA PAPQAPEVEA AAEEEAARVL
LVEDNATNQL VLRTLLQSAG CVVDAVADGA SAVSQARQVA YDVILMDLQM PVMDGLQATR
AIREGEGPNR HGRIIGLTAA VGPQFEQQCL DAGMDGYLPK PVQRSALLGL LGLRLPGSGH
//
