ID A0A0Q4RL85_9BURK Unreviewed; 1169 AA.
AC A0A0Q4RL85;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF16_16370 {ECO:0000313|EMBL:KQO15521.1};
OS Acidovorax sp. Leaf78.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO15521.1, ECO:0000313|Proteomes:UP000051234};
RN [1] {ECO:0000313|Proteomes:UP000051234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000051234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA Vorholt J.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQO15521.1}.
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DR EMBL; LMLZ01000024; KQO15521.1; -; Genomic_DNA.
DR RefSeq; WP_056172528.1; NZ_LMLZ01000024.1.
DR AlphaFoldDB; A0A0Q4RL85; -.
DR STRING; 1736237.ASF16_16370; -.
DR OrthoDB; 9796305at2; -.
DR Proteomes; UP000051234; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd19410; HK9-like_sensor; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR007891; CHASE3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 3.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQO15521.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 481..700
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 778..891
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 900..1016
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1046..1167
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 707..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 381..460
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 709..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 827
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 949
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1100
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1169 AA; 127264 MW; F673F11623CBF93C CRC64;
MPRSSSTQAT TRFAIPRTLM AGFVVAALAT LVIALVNFRA SETRGEAVAA MDRTTLAMRQ
LNLFSSALKD AETGQRGFLL TGEVSYLQPY QLALTSLERQ MTALKASTNE EPIHRRLVTQ
IDDLTRQKLR ELNETIELHK GGNRDAAMAL VRTDAGKNLM DRVRDLSSDL FTLQSQQLEA
RRQAWVDAAT MSAYYSWGGS IVLLALICAS AAMTSREYRS KSRQSWVSAG LTGLGQRLQG
DHRLEDIGKL ALEYLAGYLK ANVGAGYVAE SGGGFSLFGG YALPRERLTQ TLLADEGLVG
EAARTRTLLH VRDVPSTHLL VSSSTGQSSP AELLVAPAVE NGKVYAVIEL GFYRALDDAE
RNLMERASEM LAIAIRSGAD RTRLEALLEE TQRQSEELQT QQEELRVNNE ELEQQSRILQ
ESQAQMEVQQ TELEQTNAHL EEQTQQLEYQ REQMLRAQSA LTDKARELET ASQYKSEFLA
NMSHELRTPL NSTLILAKLL ADNKPGNLSG DQVKYAQTIY SAGNDLLALI NDILDLAKIE
AGQATVSVEP VQVGKAVQAL VEPLRLLAQE KGLALSATVA ADVPTMETDP LRLGQVLKNL
LSNALKFTEK GSITLQVSRG TGDTVVFAVR DTGIGIPAHQ QELIFEAFRQ ADGSTHRKYG
GTGLGLSISR DLAQLLGGAI SVESSAGEGS VFTLTLPARL AALQADPAAV SNSPHTAQTA
HTANAGHTAH GATPSALAPA APQLAGVVQA LSSIAAPPAA QAGGSATAVV PQRASARSIL
VVEDDERFAN ILCELAREMD FESHMAANAA DGLAMAAQLL PSAIVLDVNL PDFSGLGVLD
QLKRNPATRH IPVHVVSVAD YSQEAMGRGA VGYALKPVKR EELVQALQRL EAKFTQNLRR
VLVVEDDERQ RESVRHLLSR DDVEIVCAGT AGVALDHLRG STFDCMVMDL NLPDLTGFEL
LQQMTEQDGV SFPPVIVYTG RALSRDEEQQ LRRFSKSIIV KDARSPERLL DEVTLFLHQV
ESELSVEHRQ MLQSARSRET ALEGRNVLVV EDDVRNVFAL SSILEPTGIK LQIARNGIEA
LQALERADAS GPAVDLVLMD IMMPEMDGYT AMREIRNRPA WRRLPIIALT AKAMKDDQEK
CLAAGANDYI AKPLDVEKLL SLVRVWMPK
//
