ID A0LFW9_SYNFM Unreviewed; 753 AA.
AC A0LFW9;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sfum_0622 {ECO:0000313|EMBL:ABK16321.1};
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Thermodesulfobacteriota; Syntrophobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16321.1, ECO:0000313|Proteomes:UP000001784};
RN [1] {ECO:0000313|EMBL:ABK16321.1, 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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000478; ABK16321.1; -; Genomic_DNA.
DR RefSeq; WP_011697494.1; NC_008554.1.
DR AlphaFoldDB; A0LFW9; -.
DR STRING; 335543.Sfum_0622; -.
DR KEGG; sfu:Sfum_0622; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_020355_0_0_7; -.
DR InParanoid; A0LFW9; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR033479; dCache_1.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000313|EMBL:ABK16321.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW Transferase {ECO:0000313|EMBL:ABK16321.1};
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 DOMAIN 384..454
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 453..508
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 521..738
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 753 AA; 83748 MW; E971F99D095FE163 CRC64;
METKERLKLH RVLKIIGVVS LVMVGIAFYL GITSSRHMKG VIRGQFNDQQ LVLARTTAER
IERNIQNAIA DLTLLNSLPA VQYNDPNSYD QLLMSTMPVL YRDNIIEIRR VDRDGNTMFI
ANDQGIATGY YGVVPQEAGA YMSWASELSN RGNVMGTGAR PRDPSKDKKS IVLDLITPTR
EEAVDALHPR PSRGFAGYLK VTLDVSKLLR EIIPPIRSGK TGYAWVIDSS GNFLHHPEAS
FIGENAFEVR SSRNPAISFN DINQIQREEM LRGKEGRGTY TSGWHRDVAA PMEKLIAYSP
VRIQGPYLTY NWSVAVVAPA DEVEAEVSQI YGKQILLQGF VIFIIVLGSA SVVLHELRWS
TILEQEVALK TDDIRRYTGE LERSEAKYRS LIESAEDMIF TLDSAGVIKT ANQHMARVFG
VSGEELAGQS LFRFLPREQA TEQLDIVRKA LSSDKAQRAE SGFNLHDREL WFNIQYIPVR
EAGREHEHVL GIARDITDRK NLERQLINSE KLASLGTLAA GVAHEINNPI GIMLGFCDLM
LERMDPGTME YNDLKTIERH GLHCKSIVER LLSFARMSEE AEDRCDLNEN IQEVVSVVKH
TLDINRIRLE TALASDLPPV NIDSRGLQQV LLNLVGNAIH AMDGDGVLRI ISRTGRREED
VELIVADTGC GIRKELIAKI FDPFFTTKKV GEGTGLGLSV SYGIVSKYGG TVECASHAEE
DGPGETGTVF TVTLKTKKDA FDETTDPSVP PLG
//
