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Database: UniProt
Entry: G0HHY3_CORVD
LinkDB: G0HHY3_CORVD
Original site: G0HHY3_CORVD 
ID   G0HHY3_CORVD            Unreviewed;       431 AA.
AC   G0HHY3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Sensor-like histidine kinase SenX3 {ECO:0000256|ARBA:ARBA00039401};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=CVAR_2748 {ECO:0000313|EMBL:AEK38087.1};
OS   Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS   NCIMB 30131) (Corynebacterium mooreparkense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK38087.1, ECO:0000313|Proteomes:UP000006659};
RN   [1] {ECO:0000313|EMBL:AEK38087.1, ECO:0000313|Proteomes:UP000006659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC   {ECO:0000313|Proteomes:UP000006659};
RX   PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA   Schroeder J., Maus I., Trost E., Tauch A.;
RT   "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT   from the surface of smear-ripened cheeses and insights into cheese ripening
RT   and flavor generation.";
RL   BMC Genomics 12:545-545(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};
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DR   EMBL; CP002917; AEK38087.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0HHY3; -.
DR   STRING; 858619.CVAR_2748; -.
DR   KEGG; cva:CVAR_2748; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_11; -.
DR   Proteomes; UP000006659; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000313|EMBL:AEK38087.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:AEK38087.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          171..387
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          390..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  46579 MW;  7C5650B7095F1065 CRC64;
     MMGTPAALVL GVLLGVLVTA GVAVIVAVLR RRARERRARE EREKREAHRQ LSTIAQVMHF
     AVDAAPTAVA VVDTRQDVIL GNRMAENLGV VVERALVPEV WRLVELVFDD GDSRELVHSP
     THAGFRDRPV FSVLVRAQPL TSADDRFVVV YAWDNSENVR MESARRDFVA NVSHELKTPV
     GAISLLVEAL VESGDDPAAV GHFGARLQRE TTRMSTMIGE LITLSKLQGA ASLPDPAPVE
     VDDVIEAAVG RNREAAEMHG IELKTDAPSG ARLLGDENLL VTAVANLIAN AVNYSPEETP
     VSVSRAVKGE SVVIRVTDHG IGIAPEDQQR VFERFFRVDQ ARSRATGGTG LGLALVKHTV
     INHGGNVSLW SRPGTGSTFS LEFPVFREDA ASEPDEVPDQ ERLTATDRVG EAQMNTRRSH
     GETADAPGNS T
//
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