ID A0A0L0LBU2_9BACT Unreviewed; 681 AA.
AC A0A0L0LBU2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=evgS {ECO:0000313|EMBL:KND47483.1};
GN ORFNames=AB199_03575 {ECO:0000313|EMBL:KND47483.1};
OS Parcubacteria bacterium C7867-004.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659198 {ECO:0000313|EMBL:KND47483.1, ECO:0000313|Proteomes:UP000036787};
RN [1] {ECO:0000313|EMBL:KND47483.1, ECO:0000313|Proteomes:UP000036787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-004 {ECO:0000313|EMBL:KND47483.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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}.
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:KND47483.1}.
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DR EMBL; LFCN01000006; KND47483.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LBU2; -.
DR STRING; 1659198.AB199_03575; -.
DR PATRIC; fig|1659198.3.peg.679; -.
DR Proteomes; UP000036787; Unassembled WGS sequence.
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 Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR007895; MASE1.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KND47483.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:KND47483.1};
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 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..542
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 565..680
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 288..315
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 614
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 681 AA; 74350 MW; 471660016CA72410 CRC64;
MSAYLTHRNL FWNAVLFAAV FAAAEIFSHL YFAGGTSPAL ILPASGIALA GVIIGGPLLW
PGVFLGIFLH QLLSGSSLVI GIGIALANTL QALVGAWLLR KLGFNSFFSR VPDTIAFTVV
AVFATMIVPT VGSLALAVAG YPFPRGYVGT WMPWWIGQVL SALIVTALLV RWLPKLSVQR
TKVEWFEASA ALTSLVLVDL LLFWTPYREL GGLPLIYLIL GPLLWIALRV GPRFMTLALF
LNAVLALTGT AVMALSGGNA TELGELLFQT EIFIIMISFI FLILVSIAEE RKDTANDLRH
NVRDLEHALE RIQREDEAKS RFIATLAHEL RNPLAPLMTS LELLSLEKSP TSDTQKVAGE
MIEHVKTMRH LLDDLLDISR ISREKLTLSL EHVELHGIIA KSARTVEPLM LERRHTLTVS
LPEGAVSFEA DPIRLEQIIV NLLNNAAKYT EPGGTITLAA SIEERTLVIR VRDSGIGMDQ
AMLERVFEPF FQIEHGGRTI SGLGIGLSLT KNLVQMHGGR ISALSEGTGL GSEFVVRIPL
KEFAEKRTAA ISPTTAMESD EHRFRILVID DNRAAADGLV KLLKLRGHEA SAVYTGEEGL
AKAPEYKPEV VLLDIGLPDM EGYDVAKGLK ADERVSAVLI ALTGYGQDAD IRKAEKAGFD
YHLTKPAGLA EIEELLAKIA R
//
