MTRB_MYCTO
ID MTRB_MYCTO Reviewed; 567 AA.
AC P9WGK8; L0TF19; O05890; Q50496;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Sensor histidine kinase MtrB;
DE EC=2.7.13.3;
GN Name=mtrB; OrderedLocusNames=MT3343;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Member of the two-component regulatory system MtrA/MtrB.
CC Probably functions as a membrane-associated protein kinase that
CC phosphorylates MtrA in response to environmental signals. Probably
CC plays a role in cell division (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Autophosphorylates in the presence of Mg(2+) and/or Ca(2+), but
CC only Mg(2+) ions promote phosphotransfer to MtrA. {ECO:0000250};
CC -!- SUBUNIT: Interacts with MrtA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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DR EMBL; AE000516; AAK47685.1; -; Genomic_DNA.
DR PIR; G70592; G70592.
DR RefSeq; WP_003416988.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WGK8; -.
DR SMR; P9WGK8; -.
DR EnsemblBacteria; AAK47685; AAK47685; MT3343.
DR GeneID; 45427239; -.
DR KEGG; mtc:MT3343; -.
DR PATRIC; fig|83331.31.peg.3599; -.
DR HOGENOM; CLU_000445_89_18_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 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 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..567
FT /note="Sensor histidine kinase MtrB"
FT /id="PRO_0000428344"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 235..287
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 302..519
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 305
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 567 AA; 61619 MW; B4C73DF5D69D064E CRC64;
MIFGSRRRIR GRRGRSGPMT RGLSALSRAV AVAWRRSLQL RVVALTLGLS LAVILALGFV
LTSQVTNRVL DIKVRAAIDQ IERARTTVSG IVNGEETRSL DSSLQLARNT LTSKTDPASG
AGLAGAFDAV LMVPGDGPRA ASTAGPVDQV PNALRGFVKA GQAAYQYATV QTEGFSGPAL
IIGTPTLSRV ANLELYLIFP LASEQATITL VRGTMATGGL VLLVLLAGIA LLVSRQVVVP
VRSASRIAER FAEGHLSERM PVRGEDDMAR LAVSFNDMAE SLSRQIAQLE EFGNLQRRFT
SDVSHELRTP LTTVRMAADL IYDHSADLDP TLRRSTELMV SELDRFETLL NDLLEISRHD
AGVAELSVEA VDLRTTVNNA LGNVGHLAEE AGIELLVDLP AEQVIAEVDA RRVERILRNL
IANAIDHAEH KPVRIRMAAD EDTVAVTVRD YGVGLRPGEE KLVFSRFWRS DPSRVRRSGG
TGLGLAISVE DARLHQGRLE AWGEPGEGAC FRLTLPLVRG HKVTTSPLPM KPIPQPVLQP
VAQPNPQPMP PEYKERQRPR EHAEWSG
