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Database: UniProt
Entry: F4BQ78_CARS1
LinkDB: F4BQ78_CARS1
Original site: F4BQ78_CARS1 
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
//
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