ID G9XRD2_DESHA Unreviewed; 536 AA.
AC G9XRD2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0322_03530 {ECO:0000313|EMBL:EHL05770.1};
OS Desulfitobacterium hafniense DP7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=537010 {ECO:0000313|EMBL:EHL05770.1, ECO:0000313|Proteomes:UP000004416};
RN [1] {ECO:0000313|EMBL:EHL05770.1, ECO:0000313|Proteomes:UP000004416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP7 {ECO:0000313|EMBL:EHL05770.1,
RC ECO:0000313|Proteomes:UP000004416};
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 (AUG-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: 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:EHL05770.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFZX01000092; EHL05770.1; -; Genomic_DNA.
DR RefSeq; WP_005814241.1; NZ_JH414482.1.
DR AlphaFoldDB; G9XRD2; -.
DR PATRIC; fig|537010.4.peg.3304; -.
DR HOGENOM; CLU_000445_89_6_9; -.
DR Proteomes; UP000004416; 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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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 PANTHER; PTHR45453:SF3; HISTIDINE KINASE; 1.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHL05770.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..282
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 311..527
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 270..301
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 536 AA; 59572 MW; A899F3EC03BBCAFA CRC64;
MKQQKKSITF KLFIITSLFF IFFTSLTMLL QTVFIENFYL SKKTKDFEAN FQQFSSAYSR
LAENSTDSSA LLSEFQDKNN ASTAIINLSG STLRIFEDKR QLLLKIAKRP ASGSGPMSEI
TDDIITYNMD SKMKMLINGM RQWTSDPLAV AMVLDEGKHL IYHSGVKIDG QNSLVGIAPI
VSGGKVTGVL TAAASLQPIG EAAAVIRQFY VYFYLIALVL IFALSFIYSK IIAKPLVTLN
KTAIKLAEMD FSAKCPLNSQ DELGSLSTTL NFLSDKLDSS ISELKAANEN LKEDIEREKK
LDLMKNEFIA GVSHELKTPI SLISSYAEGI KDNITHGAKR EYYAHIIMDE SKKMASLVED
MLDLSQLESG SFKLKVEDFS LTGLLNSISE RYAGDLRRKG KNLDLSIPAY DLEVRADMFR
IEQVLTNLID NGIKYSLEGG IIKISAHDQS DTVTIEVENP GEPIPEAELP HIWSKFYRIE
KSRNKELGGT GLGLSIVREI LDRHGSAYGA ENTVSGVKFF FTLAKIKGPA EGWADR
//
