ID S7VLM2_9BACT Unreviewed; 1458 AA.
AC S7VLM2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ADICYQ_0691 {ECO:0000313|EMBL:EPR71100.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR71100.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR71100.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR71100.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(2013).
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:EPR71100.1}.
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DR EMBL; ATNM01000029; EPR71100.1; -; Genomic_DNA.
DR RefSeq; WP_020890841.1; NZ_ATNM01000029.1.
DR STRING; 641524.ADICYQ_0691; -.
DR PATRIC; fig|641524.5.peg.688; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR OrthoDB; 905895at2; -.
DR Proteomes; UP000014974; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 9.
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 NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF08448; PAS_4; 3.
DR Pfam; PF13426; PAS_9; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 8.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 8.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 634..689
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 693..735
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 952..1023
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1025..1077
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1078..1148
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1151..1203
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1232..1458
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1458 AA; 166883 MW; A18DDAA3DBADDCC2 CRC64;
MGTETEDNVF LRAGGEMGEL IRARDWENTP LGEPNSWAQP LKTMVGVLLE NPFGMYIAWG
KEYTQIYNDG YRPILGANKH PQALGSSTRE TFPEIWSIIG PMLDSVMEGE AFRFQDLMLP
LNRSGYLENC YFDFSYSPIR LATGEVGGVL VTVVETTSKK IAENDLIENK NDLEFVIEAA
QLGTYDYNPL TNTFSGNARL KEWFGLPLEE QIEYEQAIAA ISETDRDRVS QAINEVLKYS
SGGNFDIEYT IVNAVTQKEI IVHATGKTRF NEEKIAYRLN GTLEDVTDRV LASKKIEENE
RNLRLMILQA PFAISIFRGA DYTVEIANKY ALELWGRKEE EVLNIPLLEA LPEISSQGIK
ELLDGVFGTG NRFATSERPL QLLRNGILET VYVHFSYEAL YDIDGKINGI MAIGYDVTPQ
VAARKTIEES EKRYHNLIHS SPSSIAILSG KDLVITIAND IIIEYWGKGK EVIGKPYFEV
LPEMAEQGYI EVYETVYKTG TPFTSIETPV SIMQHGEMTL KYFNVNVYPQ RDLDGNIDGL
GIIATEVTSQ AIFNNKIKES EQNIRALVES APFPIGVFVG EDMSISLANQ SIMDAWGKGN
DVVGKLYSDI LPEFGNQQIF GQIRKVLQTG IPFHARNQKV DIVKDGKLKP YYYNYSFTPL
LDASGKVYAV MNTAAEVTEL HEAKQKVEEA LSEIKLFKFM ADTAADPFIL IEEDGSFAYL
NNSALEKWGY TEQEMSLLKV PDVDIIFHDK KFKEVFKRAQ REIIPPFETM HKNKQGHIYP
VEINMGGVEV DKKTMLFAIA RDITERKKAE QDVIEAFQKV EESEKRFRDS VKQAPLGIVI
FRGPENVIEI ANESYLQLID KTENQFVGKP LFETLPEVKK TIAPIIADIY RTGNAFYGYE
FPVTINRHGK TESGYYNFVY HPLKEKNVIT GIMVVVTEVT ATVTAKHIIE ENEDKLKLII
EASELGIWDL NLKTQVMVGS ERCYNILGFP NTKNLTQQEV IAHVHPDDVK LRAEAFEKAY
EVGLLHYQIR IVWEDQSLHW KDVKGKVYYD EHNKPERMLG TVRDITEERT FHQQLLEREE
KFRLLADSMP QFIWTSDPDG NINYFNQSVF DFSGLTSEQL YNDQWIQIVH PDERERNIKQ
WIQAVRSGKD FLMEHRFRKY DGEYRWQLSR AIPQKDADGA IKMWVGTSTD IQEQKMFTNE
LEKMVQLRTN ELQQKNVALE KMNKELQSFV YISSHDLQEP LRKIQIFASR ILETEYDALS
QNAQKYFTKM HKSAFRMQNL IRDLIAYSRT NDQELNYEVV ELLEIIEDTK EVLSEELEQN
NVTFELENLC NVKVVLVQFR QVIVNLVSNA IKFSRAGHAS HIRINCETVE GKKTGIESLN
DDEHYCHIRF ADNGIGFDQK YSEKIFEVFQ RLHSKDVYTG TGIGLAIVKR IIENHEGFIM
ATGELNKGAT FDIYIPQA
//
