ID W5WK64_9PSEU Unreviewed; 591 AA.
AC W5WK64;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Sensor histidine kinase MtrB {ECO:0000256|ARBA:ARBA00035305};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=KALB_7890 {ECO:0000313|EMBL:AHI01248.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI01248.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI01248.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI01248.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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; CP007155; AHI01248.1; -; Genomic_DNA.
DR RefSeq; WP_025361064.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WK64; -.
DR STRING; 1449976.KALB_7890; -.
DR KEGG; kal:KALB_7890; -.
DR PATRIC; fig|1449976.3.peg.7924; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_18_11; -.
DR OrthoDB; 9786919at2; -.
DR Proteomes; UP000019225; Chromosome.
DR GO; GO:0016020; C: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 Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 236..288
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 303..520
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 524..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 591 AA; 63659 MW; 8F4B60CB83D6BABD CRC64;
MRWFDTRSVA RWLHDAPVVV RERWQRASEL WRRSLQLRVV VSTLALSSAV VFVLGIVLQT
QITNQLLTTK IDAAVAQIKA NVGAVQHQLV GVSPGSDSLL ARFTTALNQL TSTSDGSSAG
ASAGAFEPVL ADYRSTDSTG AVTATGHFGD VPEDLKKFVQ GGQIATAIHT VPRDGGLTTM
LVVGAPVLSA THPVQLYLLF PLTAEQRTTG VVQSTLVVGG IVLLLLLAGI TNLVTKQVVR
PVRQAAEVAE RFAEGNLDDR MQVIGEDDVA RLAESYNEMA ESIQAQIHKL EEFGQLQRRF
TSDVSHELRT PLTTVRMAAD VLHASREQFP AGLSRSTELL VDELDRFEAL LGDLLEISRL
DAGVEDLTAD LVDVRGIVER AVASVSAIAG TAGSEVEIYA PEDEVPAEVD ARRVERVLRN
LLANAVDHGE GLPVRVRVAT SAEAVAITVR DFGVGLREGE AELVFNRFWR ADPSRNRRTG
GTGLGLAISV EDARLHGGWL EAWGEQGSGA CFRLTLPRVQ GVELTSSPLP LPPEDEPPVR
AEAQAEAPAE QDPVEEDEPT VAEISWQPAD SLGTTSLIGE DTPVDQHEEA R
//
