MTDRP_MYCTO
ID MTDRP_MYCTO Reviewed; 653 AA.
AC P9WLZ6; L0T6M8; Q11034;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Multidomain regulatory protein MT1410 {ECO:0000250|UniProtKB:P9WLZ7};
DE AltName: Full=Anti-sigma-F factor MT1410 {ECO:0000250|UniProtKB:P9WLZ7};
DE Short=Anti-SigF factor {ECO:0000250|UniProtKB:P9WLZ7};
DE AltName: Full=Protein-serine/threonine phosphatase {ECO:0000250|UniProtKB:P9WLZ7};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P9WLZ7};
DE AltName: Full=Serine/threonine-protein kinase {ECO:0000250|UniProtKB:P9WLZ7};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P9WLZ7};
GN OrderedLocusNames=MT1410;
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: Primarily acts as an independent SigF regulator that is
CC sensitive to the osmosensory signal, mediating the cross talk of PknD
CC with the SigF regulon. Possesses both phosphatase and kinase
CC activities. The kinase domain functions as a classic anti-sigma factor-
CC like kinase to phosphorylate the anti-anti-sigma factor domain at the
CC canonical regulatory site, and the phosphatase domain antagonizes this
CC activity. {ECO:0000250|UniProtKB:P9WLZ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P9WLZ7, ECO:0000255|PROSITE-
CC ProRule:PRU01082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P9WLZ7, ECO:0000255|PROSITE-
CC ProRule:PRU01082};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P9WLZ7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P9WLZ7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01082};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU01082};
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P9WLZ7}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK45673.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45673.1; ALT_INIT; Genomic_DNA.
DR PIR; C70742; C70742.
DR RefSeq; WP_003407159.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WLZ6; -.
DR SMR; P9WLZ6; -.
DR EnsemblBacteria; AAK45673; AAK45673; MT1410.
DR KEGG; mtc:MT1410; -.
DR PATRIC; fig|83331.31.peg.1516; -.
DR HOGENOM; CLU_030485_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.30.750.24; -; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR Pfam; PF13581; HATPase_c_2; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF07228; SpoIIE; 1.
DR Pfam; PF13466; STAS_2; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SUPFAM; SSF52091; SSF52091; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..653
FT /note="Multidomain regulatory protein MT1410"
FT /id="PRO_0000427392"
FT DOMAIN 86..142
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT DOMAIN 177..396
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT DOMAIN 546..653
FT /note="STAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00198"
FT REGION 397..544
FT /note="Anti-sigma factor kinase region"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
FT BINDING 212
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
FT BINDING 328
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
FT BINDING 387
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P9WLZ7"
SQ SEQUENCE 653 AA; 69582 MW; E6205AA55F588959 CRC64;
MAAEMDWDKT VGAAEDVRRI FEHIPAILVG LEGPDHRFVA VNAAYRGFSP LLDTVGQPAR
EVYPELEGQQ IYEMLDRVYQ TGEPQSGSEW RLQTDYDGSG VEERYFDFVV TPRRRADGSI
EGVQLIVDDV TSRVRARQAA EARVEELSER YRNVRDSATV MQQALLAASV PVVPGADIAA
EYLVAAEDTA AGGDWFDALA LGDRLVLVVG DVVGHGVEAA AVMSQLRTAL RMQISAGYTV
VEALEAVDRF HKQVPGSKSA TMCVGSLDFT SGEFQYCTAG HPPPLLVTAD ASARYVEPTG
AGPLGSGTGF PVRSEVLNIG DAILFYTDGL IERPGRPLEA STAEFADLAA SIASGSGGFV
LDAPARPIDR LCSDTLELLL RSTGYNDDVT LLAMQRRAPT PPLHITLDAT INAARTVRAQ
LREWLAEIGA DHSDIADIVH AISEFVENAV EHGYATDVSK GIVVEAALAG DGNVRASVID
RGQWKDHRDG ARGRGRGLAM AEALVSEARI MHGAGGTTAT LTHRLSRPAR FVTDTMVRRA
AFQQTIDSEF VSLVESGRIV VRGDVDSTTA ATLDRQIAVE SRSGIAPVTI DLSAVTHLGS
AGVGALAAAC DRARKQGTEC VLVAPPGSPA HHVLSLVQLP VVGADTEDIF AQE
