ID A0A0P6XAA2_9CHLR Unreviewed; 954 AA.
AC A0A0P6XAA2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ADN01_13380 {ECO:0000313|EMBL:KPL79688.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:KPL79688.1, ECO:0000313|Proteomes:UP000050501};
RN [1] {ECO:0000313|EMBL:KPL79688.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL79688.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-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:KPL79688.1}.
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DR EMBL; LGCM01000046; KPL79688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P6XAA2; -.
DR STRING; 229921.ADN01_13380; -.
DR OrthoDB; 9815750at2; -.
DR Proteomes; UP000050501; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 3.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.450.20; PAS domain; 4.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000050501};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..127
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 140..210
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 212..262
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 278..328
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 332..382
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 560..630
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 755..806
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT COILED 658..685
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 954 AA; 108280 MW; 7AB5DB621B3AA6F3 CRC64;
MTTPMSQATI ILLVEDNLID FHLIYEMLTQ LGDSRVEILH ADTLADGTQQ VNTHRVDLVL
LDLNLPDSDG LDTFIKMRQA APHAPVVVLS GVDSSELALQ AVQNGAQDYL IKGKLNADLL
MRSLRHAIER QRWEKRVRET EARYQNIFNG IRDAILVEDL NGHVLDANES ACRMYGYTRE
QILQMTAGQL APPEAFQEFD RLMQEIEATD HTMVEAPNLR ASGEIFYAEI TIQKDSLGEQ
PVLLIMVRDV SERRRTEQAY RNLVENSLQE LYIFQNRRVV YANPAAVQNS GYTLEELRAL
SPDEVRANVH PEDRARVAHN AEARMGGQNV PKLDEIRLLT KDGRTRWVAS LAVLGEYDGQ
PAIQTAQFDI TERKQVEESL RHRLAVESLI SQLSTQFINA SHDQMDAQID TALQALGEFA
GVDRCYLDIF NEDRTEIVKV YEWCAPGIQP MQDTFVGQSL KDLKWSMDTL HRFEPVYVPN
LSDLPPEADG ERQYWDTDQL TSILLLPVAF KNTLSGYVGF SNVSKPKEWD DADISMLRML
GDMLMNALQR QRADTDLRRA QEHNRLLLES IQTPVLAVDD HFHVQYCNEA FTRLFGLNPA
ELTDRSLLVY AQEIQHSIFF KAIDEAIHTG AAQTTEGWLN QRYYQVWVYP NPTGALSIAE
DLTERKQAQE ELEQARYDLH QMMASVNDAL WSGTVDKDGR LIYRYLSPVI ETITGVAYEA
LRADSRIIRP RIHPDDRDWV FQRFAELNAG QRKKSTMEFR LLNDDGSITW VRDSQTAQVM
PDGRLRLDAV VSDITEQVEA RQQLQKRLEL EALISHITTR FINVTTHSLK DQAQFALEAT
GRFADVERCY WVTFNPGGDT IQDVQEWLAA GIQPRRDRLI GLSLDTFSWA MKELRSEGIL
SVDRLENLPP GSQHRKSPVA GAGRAVHFGH CPGILRSNGG VLGPQSRTNL PPLG
//
