ID A0LI86_SYNFM Unreviewed; 1028 AA.
AC A0LI86;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sfum_1447 {ECO:0000313|EMBL:ABK17138.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK17138.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK17138.1, ECO:0000313|Proteomes:UP000001784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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};
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DR EMBL; CP000478; ABK17138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LI86; -.
DR STRING; 335543.Sfum_1447; -.
DR KEGG; sfu:Sfum_1447; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_303209_0_0_7; -.
DR InParanoid; A0LI86; -.
DR OrthoDB; 9778628at2; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0016020; C:membrane; 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; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 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; 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; IPR038318; KdpD_sf.
DR InterPro; IPR025201; KdpD_TM.
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; 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; PF13493; DUF4118; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 2.
DR Pfam; PF13426; PAS_9; 3.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABK17138.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Transferase {ECO:0000313|EMBL:ABK17138.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..193
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 212..268
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 269..325
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 343..395
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 487..539
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 625..674
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 809..1024
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 123..157
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 534..561
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 779..806
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1028 AA; 116670 MW; 1AEA6B23A44B3B14 CRC64;
MMWYRTERPI WLRLGVGVLL PVIAAVIRWH FLETLGFRAT FTTFYPAVAV AALYGRFGAG
FIATAVSALL ADYFWIEPVG QFAIAPFADR LSVAVFLANG TLISCLAEAA YRAQARAFKT
EQQSRLSAER EKAAVELQQS ERKYRELVQN ANSAIVRWNS GGTIAFFNEY AQTFFGYRED
EILGKHVSVL LPETESAGTD STALALDVVR YPERYVSIIN ENIRRDGSRV WMAWTHKAIF
DESGAVSEIL AVGTDITARR QAEEKLKHAS EFATAILDTV DGLIIVLDRN GRIVRFNAAC
ERLTGWRVDE VIGRCFWEFL VPEEQRRGVL QVFQGLTTGK FPSRHENEWI LRDGSRRWIT
WANSCLLDAK GDIVHVIGTG IDITERQRAE QALRESERLA RDQEAQIMAI LDAAPAMIWT
AHDRECRSIS GNRAARELSR VDETANMSKT GPEREHLAHY SIYKDGRELA PEELPIQVVA
STGREFRDYS LEFVLKDGPR YSLLGNVIPL IDSEGSPSGA IAAFMDITER KLMEEELRKS
RDELEIRVRE RTEELAAERQ LFFDVLETLP VYVCLLTPEY HVPFANKVFR DRFGASKGLR
CFEHLFGRSE PCEICDTYAV LKTSTPHRWE WEGPDGRSYS VFDFPFIDAK GSQLILEMGI
DVTERKQAEE ALKTERQRLF DVLETLPVMI CLLTPDHHVA FSNRSFREKF GESQGRHCYE
YRFGLNEPCN FCESYRVAET GRSHHWEVTV PDGTIIDAHD FPFIDVDGSP MILEMDFDIT
EFREAERELK ATVAKLEQLN QELQEFAFIA SHDLQEPLRK IQTFGEMLVR RKKDSLDAEG
KNLLERIIKG ANRMAELLHA LRTYSRSGTS QLIHKPVSLS EVARGAASAL EYWISKTNAK
VEIGDLPTVD ADESLLHQLF QNLISNSIKY RKESEPPVIK ISGSVIDHQC RISVQDNGIG
FDPCYSDQIF KPFQRLHGKD SPYSGTGMGL TICRKIVARH NGEITVESEP GRGSTFKVTL
PLKQQKRA
//
