ID   RSMAF_MYCTU             Reviewed;         254 AA.
AC   P9WJ65; L7N5D7;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 28.
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=Rv3912; ORFNames=RVBD_3912;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
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; AL123456; CCP46741.1; -; Genomic_DNA.
DR   PIR; H70850; H70850.
DR   RefSeq; NP_218429.1; NC_000962.3.
DR   RefSeq; WP_003400148.1; NZ_NVQJ01000005.1.
DR   AlphaFoldDB; P9WJ65; -.
DR   STRING; 83332.Rv3912; -.
DR   PaxDb; P9WJ65; -.
DR   DNASU; 886234; -.
DR   GeneID; 886234; -.
DR   KEGG; mtu:Rv3912; -.
DR   TubercuList; Rv3912; -.
DR   eggNOG; ENOG5031ZVM; Bacteria.
DR   OMA; YAVALNC; -.
DR   Proteomes; UP000001584; 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; Reference proteome; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..254
FT                   /note="Anti-sigma-M factor RsmA"
FT                   /id="PRO_0000422684"
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