ID A0A0W0GI10_9CHLR Unreviewed; 1250 AA.
AC A0A0W0GI10;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DEALK_10520 {ECO:0000313|EMBL:KTB48207.1};
OS Dehalogenimonas alkenigignens.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=1217799 {ECO:0000313|EMBL:KTB48207.1, ECO:0000313|Proteomes:UP000053947};
RN [1] {ECO:0000313|EMBL:KTB48207.1, ECO:0000313|Proteomes:UP000053947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP3-3 {ECO:0000313|EMBL:KTB48207.1,
RC ECO:0000313|Proteomes:UP000053947};
RA Key T.A., Richmond D.P., Bowman K.S., Cho Y.-J., Chun J., da Costa M.S.,
RA Rainey F.A., Moe W.M.;
RT "Genome sequence of the organohalide-respiring Dehalogenimonas
RT alkenigignens type strain (IP3-3T).";
RL Submitted (JUN-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:KTB48207.1}.
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DR EMBL; LFDV01000002; KTB48207.1; -; Genomic_DNA.
DR RefSeq; WP_058439229.1; NZ_KQ758903.1.
DR AlphaFoldDB; A0A0W0GI10; -.
DR STRING; 1217799.DEALK_10520; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000053947; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 5.
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; 3.30.450.20; PAS domain; 7.
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; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 4.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 7.
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); 7.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 6.
DR PROSITE; PS50112; PAS; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000053947}.
FT DOMAIN 7..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 210..259
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 260..330
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 339..390
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 406..461
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 464..515
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 539..567
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 589..640
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 641..694
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 712..762
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 890..942
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 961..1012
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1025..1238
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1250 AA; 138193 MW; 700D5538B82447FE CRC64;
MTVSKQKILL VTPLAADARE VNDLLARFGG ERFIIESVSQ IETALEMIEN GAHLDLLIFD
AAIADGAALD IVRAAVRRAP QVPLVVLSGE SGGAIAAEYL RAGAGEVAAL KDGGASLVQA
LDAAFERHRK EQSLRQAQRR LEAMGEVLGL GRWEILLDEM KVVASESARI IYGLEGTEWT
LSQVQAVPLL EYRAMLDRAL SELISGGQLY NVEFRIRRPN DGQTAWVQSV AEYDAAGRRV
LGIIKDITQA KNAEEALRES EHRYRLLAEK STDVIWTMSF DGRFTYVSPS VYQLRGFTPE
EVMRQSIEEA VCPDSAVVVR QGLAQAIAAA ATARTLGPAY LEIEQPRKDG GTVWTEVSVS
VVKDEGRPSH ILGVTRDITE RRRIQAELKE REAELAAIFM AEPVGIVVSV DRVIWEVNDA
ACNMCGYQRE ELVGHSSRIL YSSDADYRRL GDELYAGLES AGRVTLEMPV RRKDGSVFQA
VVSGAVLERT DLSRGIVFAI QDITERKLFE TSLKEREAKL AAIFRAAPVG IAVAVGRVIV
EANDTMYQMA GYSREDFIGR STRILYDSDA EYEKVGAELY SRLQANGHMT GEITGRRRDG
SHFPMLLSAS PLDMADLSRG IVFTAMDISE RKAAEEAIRL SEQKYRLLFN SSNDAVLFHD
EQGRFIEVND RACQILGYRR DELLGMTVAD IDDPAVILDS GVVEQMAACG SVVFEQVHVA
KDGRRIPVEI SSRQIQLGGR QMVLSVARDI TERKKAEAEL RRSMSLLAAT LEATADGILV
VGLDGKVQRY SSRFAKMWGI PKSLLAKGDD NALLDNVLSQ LAEPQQFLDK VHELYAHPSR
SSFDTLLFKD GRVFERYSRP QKIGEQIVGR VWSFRDVTQH QTMEDRLLRA AEEWRATFDA
ISTPVSIQDR DFKILRVNKA YAESLNTTAE ELIGKTCFEV SHGTGEPVEN CPHLRTLDSG
QPAEVEIHNA AKGTYTVVST YPMFGPAGEV VATVHIAQDI TERKKMQEKL MVTNRLASVG
ELAAGIAHEI NNPLTGVLGF SELALSADLP QSVRADIEVI HSEARRAADV VKNLLIFARR
HQQARAPLSI NDVISRTLAL RAYEQKIHNI EMITDLEQEL PEITADYFQL QQVFLNIIIN
AEFFMIQTHN RGRLVVTTRF LPGERVIRVS FADDGPGIPA DVLPRLFDPF FTTKEVGQGT
GLGLSISHGV VQSHGGRIWA ESQQGAGATF FIDLPLRPPE SSPEQAGIIV
//
