MTRB_MYCBO
ID MTRB_MYCBO Reviewed; 567 AA.
AC P59963; A0A1R3Y3J3; X2BNF3;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Sensor histidine kinase MtrB;
DE EC=2.7.13.3;
GN Name=mtrB; OrderedLocusNames=BQ2027_MB3273C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Member of the two-component regulatory system MtrA/MtrB.
CC Seems to function as a membrane-associated protein kinase that
CC phosphorylates MtrA in response to environmental signals (By
CC 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; LT708304; SIU01902.1; -; Genomic_DNA.
DR RefSeq; NP_856918.1; NC_002945.3.
DR RefSeq; WP_003416988.1; NC_002945.4.
DR AlphaFoldDB; P59963; -.
DR SMR; P59963; -.
DR EnsemblBacteria; SIU01902; SIU01902; BQ2027_MB3273C.
DR GeneID; 45427239; -.
DR PATRIC; fig|233413.5.peg.3600; -.
DR OMA; NRFWRSD; -.
DR Proteomes; UP000001419; 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_0000074806"
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
