GenomeNet

Database: UniProt
Entry: A0A0C5G266_9ACTN
LinkDB: A0A0C5G266_9ACTN
Original site: A0A0C5G266_9ACTN 
ID   A0A0C5G266_9ACTN        Unreviewed;       692 AA.
AC   A0A0C5G266;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Sensor histidine kinase MtrB {ECO:0000256|ARBA:ARBA00035305};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TU94_13115 {ECO:0000313|EMBL:AJP02279.1};
OS   Streptomyces cyaneogriseus subsp. noncyanogenus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP02279.1, ECO:0000313|Proteomes:UP000032234};
RN   [1] {ECO:0000313|EMBL:AJP02279.1, ECO:0000313|Proteomes:UP000032234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP02279.1,
RC   ECO:0000313|Proteomes:UP000032234};
RA   Wang H., Li C., Xiang W., Wang X.;
RT   "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT   Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP010849; AJP02279.1; -; Genomic_DNA.
DR   RefSeq; WP_044381911.1; NZ_CP010849.1.
DR   AlphaFoldDB; A0A0C5G266; -.
DR   STRING; 477245.TU94_13115; -.
DR   KEGG; scw:TU94_13115; -.
DR   PATRIC; fig|477245.3.peg.2777; -.
DR   HOGENOM; CLU_000445_89_18_11; -.
DR   OrthoDB; 9786919at2; -.
DR   Proteomes; UP000032234; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AJP02279.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032234};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        73..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        264..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          284..336
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          351..568
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          567..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   692 AA;  73049 MW;  837DF8FF8CC3DF98 CRC64;
     MSGDSAASVP GRSGARAGRP VGRKAGGSRG RRFLEGGLLH GGVQGSPVLR LFMRWVRRPL
     LPVIRLWRRN LQLKVVVTTL LMSLGVVLLL GFVVIGQVRN GLLDAKVKAS QSQATGGFAA
     AKQRADEAAT AAGDAGTPVD DRPSQNVIQW MSDLVYSLSS GGQGAFDVVT LPAVGDSGGG
     RGPRASGDVA PSASIPESLR ERVDSSTAAA QSYTRIVYNS SEASQPALVI GKRVNDPNGD
     PYQLYYLFPL TQEEKSLSLV KGTLATAGLF VVVLFGAIAW LVVRQVVTPV RMAAGVAERL
     SAGRLQERMK VTGEDDIARL GEAFNKMAQN LQLKISQLED LSRMQRRFVS DVSHELRTPL
     TTVRMAADVI HEAREDFDPV TARSAELLAD QLDRFESLLA DLLEISRFDA GAAALEAEPI
     DLREVVRRVV SGAEPLAERK GTRIRVTGDQ QPVVAEADAR RVERILRNLV VNAVEHGEGR
     DVVVKLAAAG GAVAVAVRDY GVGLKPGEAS RVFSRFWRAD PARARTTGGT GLGLSIALED
     ARLHGGWLQA WGEPGGGSQF RLTLPRTADE PLRGSPIPLE PADSRGRRAA EEAAPAGGGA
     KGATVPAQQS AGSGHARPAR DPIPPRPAAA SPAADPTALP GNGARVVPRP VSPARRQDGP
     STAEPSAAHG GEHPADRPEE DPNSQGEACR GR
//
DBGET integrated database retrieval system