ID F4BQ78_CARS1 Unreviewed; 584 AA.
AC F4BQ78;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=yesM {ECO:0000313|EMBL:AEB30928.1};
GN OrderedLocusNames=CAR_c22710 {ECO:0000313|EMBL:AEB30928.1};
OS Carnobacterium sp. (strain 17-4).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=208596 {ECO:0000313|EMBL:AEB30928.1, ECO:0000313|Proteomes:UP000008304};
RN [1] {ECO:0000313|EMBL:AEB30928.1, ECO:0000313|Proteomes:UP000008304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-4 {ECO:0000313|EMBL:AEB30928.1,
RC ECO:0000313|Proteomes:UP000008304};
RX PubMed=21551290; DOI=10.1128/JB.05113-11;
RA Voget S., Klippel B., Daniel R., Antranikian G.;
RT "Complete gnome sequence of Carnobacterium sp. 17-4.";
RL J. Bacteriol. 193:3403-3404(2011).
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; CP002563; AEB30928.1; -; Genomic_DNA.
DR RefSeq; WP_013711870.1; NC_015391.1.
DR AlphaFoldDB; F4BQ78; -.
DR STRING; 208596.CAR_c22710; -.
DR KEGG; crn:CAR_c22710; -.
DR eggNOG; COG2972; Bacteria.
DR HOGENOM; CLU_020473_6_1_9; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000008304; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AEB30928.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 21..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 474..576
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 359..386
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 584 AA; 66601 MW; 83B2DD63480587C4 CRC64;
MSQIIKKTIK TITDKFKSLR IILALSLGVI SIFTILLFAG FLSVTFKETL IATTKTTTQQ
SVVQSSITLA NEIDNMTRMA YGILDELKSS TLQKNEIANL LGVSYRLNRN IVSIGLINAN
GQLVDYAPSQ YTLKKELKIY EQDWFQEDLK PNQFSFSLPH VQNIFEKNDR WVLSGTAPVI
VDKEEYLLLI DFNFNSIGNY FDKVSIGKRG YSFILDSQNA LVYHPKQQIR QTNAKEENLD
FIADKSDGVY ITPNKENVIA VASVSSTGWK VIGVSYLQES IKEAMQEVQR YMLWVFLAIV
SLVVLISIGV SKYIAQPITK MVKVMRNSDK DQFDIYTDET RFTEIQQLSG SYNYLIDHVK
MLMLQVKEEQ EELRKSEMNV LQAQINPHFL YNTLESILWM SERGNNEGAS EMVAALGKLL
RISLSKGNDF ISLRQELAHA ESYLTIQQIR YKNQFQYSIE ADDTILDCLT VKIILQPFLE
NALYHGIERM VDEGNIGIKV FDKQDKILIQ ITDDGIGILP ETLKEIEAGK NSEKVGIGIR
NVHQRIQIYF GKDFGVEVTS EMDEGTMISI WLPKIVRGED QKEK
//