ID M0ICD9_9EURY Unreviewed; 1301 AA.
AC M0ICD9;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C452_02125 {ECO:0000313|EMBL:ELZ94455.1};
OS Haloferax alexandrinus JCM 10717.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1227458 {ECO:0000313|EMBL:ELZ94455.1, ECO:0000313|Proteomes:UP000011577};
RN [1] {ECO:0000313|EMBL:ELZ94455.1, ECO:0000313|Proteomes:UP000011577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10717 {ECO:0000313|EMBL:ELZ94455.1,
RC ECO:0000313|Proteomes:UP000011577};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:ELZ94455.1}.
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DR EMBL; AOLL01000004; ELZ94455.1; -; Genomic_DNA.
DR RefSeq; WP_004062124.1; NZ_AOLL01000004.1.
DR GeneID; 44083356; -.
DR PATRIC; fig|1227458.3.peg.391; -.
DR Proteomes; UP000011577; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; 5.
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; 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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
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; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELZ94455.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..129
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 144..214
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 258..294
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 634..686
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 687..764
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 818..887
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 890..942
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1107..1301
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1301 AA; 144985 MW; 0A0E9993157ED161 CRC64;
MLGTSDELDD PIHVLYVNSD PAFAELVQTK LQQTSTEIDC IPADGIDEAL QHLATERIDC
IVTAYSLEDS DGIGFTESIR QQNDDIPILL FTGQGSEEIA SKATRAGVSD YIPVRSERDN
FTLLAARIRT LTRAARKQTE AEQTKRRFRR TLERATDAIY AVDSDWRIEY MNEKMAERIG
RDPDALVGEA IWEEFPSIVG TELEDKYRTA METGEPVSFE QHLEEPFNYW VEVRAFPDDD
GLTVFSREIT TERERELKLE RSDAILENIH DVVFVLDEQG DIEFANTAAK RLLAGEQSAQ
LTGQQLETVV GDRVSNSDIT RFSQAVESTL DEIESDGGST GLYDADLQLD VVVGISERTF
DVRVTPFQSR KSKQVLVVAR DVTEQSEVKR QLERERDALQ DLQAVMAESD VSAESRLQNL
LEVGCQTLGL EIGIVSRIQD SDYTVEAAHA PEADIEAGDQ FDLESTYCAE VVGTDSVCSF
VDAVSDGKET HPAYRDFELE SYIGVPLVVD DTRYGTVNFS SPTTRVAPFG ALERTFVELV
AQLVSTEISR RRDHTELERQ GFLFDRVQDI ADVGIWEFIP SSGELMWSDG VRQIHRVDED
YEPSLDDAIE FYHPDDRETI TAAVDRAIED GEPYDLDLRI VRTDGEVRHV RAWGEYVEDT
PRGDAVLRGV FQDITEREAE RHQYRELAEE YEALLETSGD AIFLLDVDTA GEDPSFKFAR
LSPGYETQTG LTTEEVRGKT PREVFGDEQG AELEANYTRC VEQRAPISYR EELDIGEDAR
FWETSLAPVV VDGETVRVVG IARNVTEQVE RERELEATNQ RLESLIEATP LTVMEIDTDG
TVIRWNDEAE TMFGWSQDEV LGEFNPMVPD EQQEEFVSHR ERVLNGERIR AKEIRRETKD
GDELDLLLSV APVTGPDGET TSILAVLEDI TEQKRLEARL RSLQETARSL SGAESSDEIG
AIAVDAAAEI LDLDITGIWE YDDRENVLAP ITETSEARDL FGESPRFTPG DSLAWDVFES
GETQVYDDIQ AEGQPHNPNT EIRSEILVPL GEYGLMSTGS VSTQVFSETD VDLFRILGAT
VEAALARASR EAELRRQNER LDQFASVVAH DLRNPLSVAM GFLEIAEETG KAEHFEKVES
AHDRIERLIE DLLTLARGET AIEDAEEIDL ESITTEAWGY VDTEEATLTV ADGIPTVTGD
AGRLTQLFEN LFRNAIEHGG ADVTVTVGGL DGDDGFYVED TGSGIPQEKQ DDVFKHGVTS
SEGGTGFGLS IVADIAKAHG WTVSVTDGSN GGARFEFKRS K
//
