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Database: UniProt
Entry: M1P0E5_9CORY
LinkDB: M1P0E5_9CORY
Original site: M1P0E5_9CORY 
ID   M1P0E5_9CORY            Unreviewed;       499 AA.
AC   M1P0E5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=A605_11250 {ECO:0000313|EMBL:AGF73250.1};
OS   Corynebacterium halotolerans YIM 70093 = DSM 44683.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1121362 {ECO:0000313|EMBL:AGF73250.1, ECO:0000313|Proteomes:UP000011723};
RN   [1] {ECO:0000313|EMBL:AGF73250.1, ECO:0000313|Proteomes:UP000011723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 70093 {ECO:0000313|EMBL:AGF73250.1};
RX   PubMed=23408721;
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Niehaus K., Szczepanowski R.,
RA   Kalinowski J.;
RT   "Genome sequence of the halotolerant bacterium Corynebacterium halotolerans
RT   type strain YIM 70093(T) (= DSM 44683(T)).";
RL   Stand. Genomic Sci. 7:284-293(2012).
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; CP003697; AGF73250.1; -; Genomic_DNA.
DR   RefSeq; WP_015401666.1; NZ_JIAJ01000003.1.
DR   AlphaFoldDB; M1P0E5; -.
DR   STRING; 1121362.A605_11250; -.
DR   KEGG; chn:A605_11250; -.
DR   PATRIC; fig|1121362.3.peg.2281; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_6_11; -.
DR   Proteomes; UP000011723; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          211..263
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          271..482
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   499 AA;  53822 MW;  BC58A7000F64638F CRC64;
     MKLPSPRLPS GYPSASLRWR IVLWITVVVL VTLASVIVIT RSVLLSQVTN TANAAVEQEI
     EEFRRFAQEG TDPATAQPFG SAARLIEVYL ARQIPDDNEA IFGLVDDQLI QMDLSGIGGT
     HPEPLSSTEP LVREIATSAA TAGVVTDDER GPAHWGRVNV STGPEDPESH FAVIAFTKDH
     RTAVDAEVRL ISLVALGGLA ASVLIAWLIA GQIIAPIRQL RNVSSRISNS DLTRRVPVEG
     NDEIAQLAET FNAMLDRLEA AYRDQRQFVD DAGHELRTPI TVVRGQLELL ESSPPEERAR
     SIELATAELD RMARMVNDLL FLAVADSGDF VHPAEVDAAE LTIDIEDKAQ TISDRIQLVA
     VAEGTVTLDE QRITEAVLEL MGNALRYSGD GVGLGSEFIG EGTGRVFRIW VRDRGPGVPA
     EQQDVVFSRF SRGEQTGTNR PSGAGLGLSI VQAIGEAHGG RAYVDSTVGL GSIFGLEIPA
     PETGAGTVTE TDRMRKEQK
//
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