ID A0A1Q8YKG3_9BURK Unreviewed; 1996 AA.
AC A0A1Q8YKG3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=chpA {ECO:0000313|EMBL:OLP08538.1};
GN ORFNames=BLL52_0145 {ECO:0000313|EMBL:OLP08538.1};
OS Rhodoferax antarcticus ANT.BR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP08538.1, ECO:0000313|Proteomes:UP000185911};
RN [1] {ECO:0000313|EMBL:OLP08538.1, ECO:0000313|Proteomes:UP000185911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANT.BR {ECO:0000313|EMBL:OLP08538.1,
RC ECO:0000313|Proteomes:UP000185911};
RA Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M.,
RA Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J.,
RA Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J.,
RA Sattley M.;
RT "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple
RT nonsulfur bacterium from an Antarctic microbial mat.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the transmission of sensory signals from the
CC chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC can transfer its phosphate group to either CheB or CheY.
CC {ECO:0000256|ARBA:ARBA00035100}.
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:OLP08538.1}.
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DR EMBL; MSYM01000001; OLP08538.1; -; Genomic_DNA.
DR RefSeq; WP_075584812.1; NZ_MSYM01000001.1.
DR STRING; 81479.RA876_14805; -.
DR Proteomes; UP000185911; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 2.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 4.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OLP08538.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000185911};
KW Transferase {ECO:0000313|EMBL:OLP08538.1}.
FT DOMAIN 660..764
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1012..1110
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1212..1314
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1463..1696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1698..1834
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1873..1989
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 983..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1404..1431
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 707
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1054
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1259
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1922
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1996 AA; 216591 MW; 9C316D37EA149F8B CRC64;
MPSAAPTSDI TNLEPDLGPL AWVLDELRKS LDGATQALRR FVRDAELSRG SDIAALDASQ
LRIARQQLHQ AVGALEMVGL EVPARMLRAM EALVNKFVQR PEFCSDEAAQ KVERASFALT
DYLEAVLKGK TLSSVALFPQ YRDVLALTND DRIHPADLWA YDWHWLDVSV PPQARRLPYD
AAVRSRIDGS ILNVVKTGHS PSALALRDIS MGFAANQTDL NPRVWWMVCA AYFEVVAFHL
CASDLYEKRA ATRVLLQYRT LARGEPEISE RLVRDLLFFC AQAALSPEHD TPALRAVHLA
YDFASPVHID YDKPQFGRFD PAVLAQARKR VATATETWSS LSGGDVSRIK AAADQFGMVA
DSIVKLHPDN VELAAALLRA MDSVSRSGMA PPVGLAMEVA TAVLYLEAAY EDRDPDSAQT
VQRGSRLAQR LDRVLSGAQP EPLDTWMEEL YRRVSDRQVM GSVVDELRTT LGEVESSLDA
FFRRPEDKVP LHEVPGRLAQ MRGVFSVLGL DQAALATLRM RASVERFLIS QVDEPQAHKA
VFDKLGNSLG ALGFLIDMLS YQRELAKKLF VYDEQEGEFR SVMGRQKGPA EVVAELSPAA
PELTASAPVV AATPQTATAP QALAPQAPAP QAPAPPTVMT PVPASVARQP PVVAVEEDDD
GDDDVELRSI FMEEAREVIQ TGLGAVGALH DNPSDMEQLT GLRRSFHTLK GSSRMVGLNE
FGEAAWAMEQ VFNAWLPQQS PASPALVKLA QQALQGFSHW VNAIDANQDE SLRALPFRRA
GDSLRLDGMG GELALPGVAV PLELPAPTAP VAEVPQDCAL LTAPVEGLED VEALVPAELA
QDRVELLPVL LEQAPEELLA EWPELAADAE PGPAAERRDF LATQINDFSD TQMVDFSETL
MSNFGDFSAP ETVPDFPELA PAIEMAELPK LADLADKPVL TETVELTELT ETEFVEKAAP
ETVKEAALPI ELLLPEVDAV TALPEPEPEP EPEPEPESAE EQVKTIGSLR IGIPLYNVYL
NEADEWSRRL LTELNEWSLE LEHPVPDSAV GLAHSLAGSS ATVGFMDLSE MARALEHALE
HTRLGVTGLP EHAQLFVDAA EDIRRLLHQF AAGFLKHPDP ELLLALKAVL ETDLSSQVAL
EDAWLDERPT EPEFEPEMDL DLDFGDLLAP TSPELPGLPQ VPDIAPAIVP EPEPLSPATE
PLASVPEPLD ARDLLDVDLF PIFEEEALEL LPKLSGALRQ WSVHPDNLSA RQEALRILHT
LKGSARLAGA MRLGEMAHRM ESAVERIDAE AAQSNQIEPL LARLDAITDC FEALRATPLA
ELVLPEVAET VPAELSQMTA EPADESAAPA LEAAAAPLQL SALTEAPLRR ASNQSIRVKS
QLIDRMVDQA GEVMISRSRL ASRLGQLRGS LDELTSNLSR LRSQLRDIEV QSESQMQSRM
AQTKDAEQSF DPLEFDRFTR VQELTRMMAE SVHDVATVQR NLQQAVEGVE DDLAAQARQT
RDLQRDLLRT RMVEFDSVAE RLYGVVRQAS KDFDKPVRLD IGGGSLEMDR GVLDRAVPAF
EHILRNAVGH GIEPAPTRKA AGKPEMGVIT LHVEQQSNDV AVTFSDDGAG LNLAGIRAKA
LANGVMGADS TLSDEQVANL IFTSGLSTAT EVSEMAGRGI GMDVVRNEVN ALGGRVELST
QAGQGTEFKL VLPLTTAVNQ VVLLRLGEVV VGVPANQVEL IRRVPVAVLN EAYKAGTFDY
NGQALAFYWA GALLQTSPVS SEPHVKTAPI AILRSAGQFV ALHVDEVLGN QEVVVKNLGP
QLSRLPGLAG MSALASGAVV LIYNAVALAG AYGAQAHAYT SAHAVAPAQA ASVAAGTTGA
LPTPAVAVNQ VPLVLVVDDS ITVRRVTQRL LKREGYRVAL AADGLQALEQ LQLEKPAVVL
ADIEMPRMDG FDLVRNIRAD DLLKDLPVIM ITSRIAEKHR EYARALGVNH YLGKPYPEDE
LIALVRGYCD AHLSVK
//
