RSMAF_MYCTO
ID RSMAF_MYCTO Reviewed; 254 AA.
AC P9WJ64; L7N5D7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Anti-sigma-M factor RsmA;
DE AltName: Full=Regulator of SigM;
DE AltName: Full=Sigma-M anti-sigma factor RsmA;
GN Name=rsmA; OrderedLocusNames=MT4031;
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: An anti-sigma factor for extracytoplasmic function (ECF)
CC sigma factor SigM. ECF sigma factors are held in an inactive form by an
CC anti-sigma factor until released by regulated intramembrane proteolysis
CC (RIP). RIP occurs when an extracytoplasmic signal triggers a concerted
CC proteolytic cascade to transmit information and elicit cellular
CC responses. The membrane-spanning regulatory substrate protein is first
CC cut extracytoplasmically (site-1 protease, S1P), then within the
CC membrane itself (site-2 protease, S2P, Rip1), while cytoplasmic
CC proteases finish degrading the regulatory protein, liberating the sigma
CC factor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ECF RNA polymerase sigma factor SigM; this
CC should inhibit the interaction of SigM with the RNA polymerase
CC catalytic core. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The cytosolic domain interacts with sigma factor SigM.
CC {ECO:0000250}.
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DR EMBL; AE000516; AAK48396.1; -; Genomic_DNA.
DR PIR; H70850; H70850.
DR RefSeq; WP_003400148.1; NZ_KK341228.1.
DR AlphaFoldDB; P9WJ64; -.
DR EnsemblBacteria; AAK48396; AAK48396; MT4031.
DR KEGG; mtc:MT4031; -.
DR PATRIC; fig|83331.31.peg.4337; -.
DR HOGENOM; CLU_080969_0_0_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.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Anti-sigma-M factor RsmA"
FT /id="PRO_0000427884"
FT TOPO_DOM 1..112
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 254 AA; 25769 MW; 986EF457CDF41B0C CRC64;
MSAADKDPDK HSADADPPLT VELLADLQAG LLDDATAARI RSRVRSDPQA QQILRALNRV
RRDVAAMGAD PAWGPAARPA VVDSISAALR SARPNSSPGA AHAARPHVHP VRMIAGAAGL
CAVATAIGVG AVVDAPPPAP SAPTTAQHIT VSKPAPVIPL SRPQVLDLLH HTPDYGPPGG
PLGDPSRRTS CLSGLGYPAS TPVLGAQPID IDARPAVLLV IPADTPDKLA VFAVAPHCSA
ADTGLLASTV VPRA