ID A0A1W9KRX7_9BURK Unreviewed; 1259 AA.
AC A0A1W9KRX7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BWK72_16490 {ECO:0000313|EMBL:OQW86679.1};
OS Rhodoferax ferrireducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=192843 {ECO:0000313|EMBL:OQW86679.1, ECO:0000313|Proteomes:UP000192505};
RN [1] {ECO:0000313|EMBL:OQW86679.1, ECO:0000313|Proteomes:UP000192505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A7 {ECO:0000313|EMBL:OQW86679.1};
RA Sharrar A.M., Flood B.E., Bailey J.V., Jones D.S., Biddanda B.,
RA Ruberg S.A., Marcus D.N., Dick G.J.;
RT "Novel large sulfur bacteria in the metagenomes of groundwater-fed
RT chemosynthetic microbial mats in the Lake Huron basin.";
RL Submitted (JAN-2017) 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:OQW86679.1}.
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DR EMBL; MTEI01000014; OQW86679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9KRX7; -.
DR Proteomes; UP000192505; 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; cd00130; PAS; 2.
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; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 4.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..286
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 366..412
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 437..491
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 513..550
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 565..619
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 892..1113
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1138..1256
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 1189
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1259 AA; 139506 MW; 56440F79ADC86CE2 CRC64;
MVDNDFLWQV HRISTHLEFM KAGFKRRFNA GLGVPLGLFV LGVVISTAGV FWLNERHLTQ
SHIDYQRLVE RVASEITRRV TLPVSGINGL RAMYVASDEV TRKEFTTHVF SRDLPNEFPG
VRGFAYVERV QREALEGFLT RVRADDAPEF AVRTIQADQP DPLYVVTFIE PAVDNGGAQG
LDVGSEPRRR NAIEYAVDSA APIMTAPVLL VQNLQQTPGA IIYVAVYREA ARLNSAMERR
SALRGLISAP IVFKELLGDL DLVSNNALVI RLTDITNGQA ANNLLFENEL LSGGRFQSSQ
TLNLLGRQLS LQTHSTAFLI AGRDSFQPWL IGLGGILSSA LLALLLWQQA HGRQRAETLA
QNMTQDLNRL ALVARNTSNS VVITDAQRRI TWVNPGFERI TGYQANEVIG KSPSFLQFEA
TDRNTIAQMH DAFEAGRGFQ GEVLNRSKQG VDYWLSMDIQ PLHEPDGKLS GFVGVQTDVT
ERKSTQSQLE GLLRDNSALM STLDLFCIVS TADRDGNITS ANDAMCDISG FSLEELLGQN
HRLFNSGVHP TTFWQDMWQK IATGRSWRAE ICNRTKSGSL FWVDTFIAPF IGDDGLVDKL
VAIRIDITAR KQAEAKLRWN QSLLQMMSNS SPLGFLVVDD RDDRILYFNA RFCEIWGASH
LAGPMQRGEI NNHSLMAKCQ SVLLDPAAFN ATWVPLQDAT NRATLEDEIT FTHGRTIRRF
STQIRDEADQ YFGRFYLFED ITERRTIEAQ AQRNAELLRG SIDALSDAFV LYDDQDRLVM
FNQPYRDLYT LAADQIVIGN RFEDVVRAGL ERGQYVNALG REDAWLAERL AQHRQPESQL
IEKLVSGRTV RIVDRRMPNG YTVGFRMDIS ELVRATEAAE EASRSKSQFL ANMSHEIRTP
MNAILGMLTL LRKTQLTPKQ ADYANKSEGA AQSLLGLLND ILDLSKVESG KMTLDPHPFA
LAQLMTDLEV IMAAYIGQRP VQLVLDMAPQ LPAFLVGDAL RLKQVLINLC GNAIKFTPQG
LVTLSIHEID RSHGKIQLKF AVQDQGIGIA PENQARIFSG FTQAEASTTR RYGGTGLGLA
ISQKLITLMG GQLELSSALG QGSQFYFNIP LALAPGMAPT LAVPHPPGQP GARLKGWRIL
VAEDNFVNQQ IATELLQGEG AAVVMVNNGQ DALNAVASAD QPFDVVLMDM QMPVMDGLSA
TRQLRQRHDA AALPIVAMTA NAMDSDREAC LQAGMNDHVG KPFNMAHLVQ VLHRAKAPP
//
