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Database: UniProt
Entry: F8E0Z5_CORRG
LinkDB: F8E0Z5_CORRG
Original site: F8E0Z5_CORRG 
ID   F8E0Z5_CORRG            Unreviewed;       577 AA.
AC   F8E0Z5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Sensor histidine kinase MtrB {ECO:0000256|ARBA:ARBA00035305};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=mtrB {ECO:0000313|EMBL:AEI10074.1};
GN   OrderedLocusNames=CRES_1722 {ECO:0000313|EMBL:AEI10074.1};
OS   Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS   158).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI10074.1, ECO:0000313|Proteomes:UP000000492};
RN   [1] {ECO:0000313|EMBL:AEI10074.1, ECO:0000313|Proteomes:UP000000492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC   {ECO:0000313|Proteomes:UP000000492};
RX   PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA   Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA   Schneider J., Trost E., Tauch A.;
RT   "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT   human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT   samples of a leukemia patient.";
RL   BMC Genomics 13:141-141(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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP002857; AEI10074.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8E0Z5; -.
DR   STRING; 662755.CRES_1722; -.
DR   KEGG; crd:CRES_1722; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_18_11; -.
DR   Proteomes; UP000000492; 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; IPR047669; MtrAB_MtrB.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; NF040691; MtrAB_MtrB; 1.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 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, ECO:0000313|EMBL:AEI10074.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000492};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEI10074.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        57..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          249..301
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          316..533
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          543..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  62660 MW;  8C9F29AD98171DAF CRC64;
     MTAEQKKAPG TAVAVSAPEP QSSKELWRGF ARRPVTTVRR AVDYFAQRWQ NSIQLRVIGS
     VLLASLLVTV ILGFVLISFV GQQLLNTKYS AATEELDRAR VAVEEQINSS DASNPVDVRL
     SSALAVLSER SGGVDQSSAA VYDPVLIARG VNDGETIAPP SARIPDELRR FVQQGQVAYQ
     YETFSGQNGN YKALVIGTPV SSELSGLELY LVMPLEAEET TLSLMRGLLT AGAIVLLVLL
     VVIAWVFSQQ LTTPVRTASR IAERFAAGHL RERMVVTGND EVARLALSFN DMAEKLSTQI
     RNLEEFGSLQ RQFTSDVSHE LRTPLTTVRM AADLINDSAE NLDPLTARAA SLMNKELDRF
     ETLLGDLLEI SRHDAGVANL SREKVDARGV VRSALAQVHV IAEEIGTTLE VDLPEEPVMV
     EIDSRRVERI LRNLFANAVD HSEGKPVNVT MAVGKTALAV TVVDHGVGLK PGEEDLVFNR
     FWRSDPSRER RTGGTGLGLA IAQEDARLHG GRLEAIGEPR VGACFRLTLP LVAGNQTAES
     PLPLEVDHSF VSDAHEGAED DPDRAAQGVE PKKSEKG
//
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