ID A0A0Q4XZ60_9BURK Unreviewed; 1140 AA.
AC A0A0Q4XZ60;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF43_09105 {ECO:0000313|EMBL:KQP18468.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP18468.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP18468.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP18468.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP18468.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP18468.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
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:KQP18468.1}.
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DR EMBL; LMMV01000012; KQP18468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4XZ60; -.
DR STRING; 1736316.ASF43_09105; -.
DR Proteomes; UP000051560; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-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; 1.10.4160.10; Hydantoin permease; 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; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 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; 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 PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000051560};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 388..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 427..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 608..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 689..908
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 935..1051
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 655..689
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 985
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1140 AA; 124871 MW; B49D568AC206A276 CRC64;
MDAAPQRIVK VRRDYNSWVA RETMEDYALR FTPQRARKWS EWRVANTAFG AASFLILEAV
GATLLVQYGF INAFWAIVAT GLIIFLAGLP ISIYAARYGL DMDLLTRGAG FGYIGSTLTS
LIYASFTFIF FALEAAVMAY ALELALGIPP TWGYLVCAVV VIPLVTHGVA AISRLQVWTQ
PLWLVMLVVP FVYVLMRDPG AFAGVTHYVG DKASHLGFDV NLFGAALTVG IALITQMGEQ
ADYLRFMPVR TAANRRKWWF GVLAGGPGWV VLGVVKMLGG ALLAYLAITH MVPKDRAVDP
NQMYLAAYEY VFPHYGWAVA ATAVFVVVSQ LKINVTNAYA GSLAWSNFFS RVTHSHPGRV
VWVVFNTLIA FMLMEMNVFQ ALGEVLGLYS NLAIAWIMAV VADLVVNKPL GLSPQGIEFK
RAHLYDINPV GVGAMALASV LSISAYLGAF GPTAQAFSAL IALGTAFVAS PLIAWAMKGR
YYIARTSDAT GHRARHCVIC EREYEGPDMA HCPAYQGPIC SLCCTLDARC GDLCKPRASL
SWQWSTALRW LLPRRIWPYL DTGLGHFLLL MLVVVPLLAA VFGLLYSQET AVVEDAALRL
AEDALRSGFV KAYMALLLIA GIVAWWFVLA HKSRQVAQEE SNRQTHLLMR EIESHRQTDA
ALQQARQVAE RARQQADQAN QAKSRYISAI SHELRTPLNS ILGYAQLMGE DQAVPPHRKH
AVHVIRRGGE HLLQLIDGTL DIARIESGKL TLTMKPLAFA DTVNEVAALF ELQAQDKGLA
FHFEAEGALP EVVRADEKRL RQILINLLGN AIKFTAAGHV RFRVRYQREM AVMEIADTGP
GIAPDALARI FEPFERAAHV ASPGPAAPGA GLGLTIAKML TDLMGGELTA SSQPGEGSVF
KVRLFLPELH GTAGRPVAKP APVAPRRGYA GTRRRILVVD NEEADRELLV HLLEPLGFEL
RMAASGHDCL DLLVAGYRPD AILMDLAMPG IDGWETVRRL RALLPEPPRV AIVSANAFDK
GLENDVGIRP EDFMVKPVRH SELLDWLGRQ LALTWLEQLP TPASAAAPQI AALVYPAPAH
LDALQGAVDL GFVRGIANQL DLIAREQPEC AGFTEKMRAL ARQFQFEAMG RLLNDAPRSA
//
