RSMAF_MYCTE
ID RSMAF_MYCTE Reviewed; 254 AA.
AC H8F2P5;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 25-MAY-2022, entry version 34.
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=ERDMAN_4292;
OS Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=652616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=22535945; DOI=10.1128/jb.00353-12;
RA Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL J. Bacteriol. 194:2770-2770(2012).
RN [2]
RP PROBABLE CLEAVAGE BY RIP1.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=20545848; DOI=10.1111/j.1365-2958.2010.07232.x;
RA Sklar J.G., Makinoshima H., Schneider J.S., Glickman M.S.;
RT "M. tuberculosis intramembrane protease Rip1 controls transcription through
RT three anti-sigma factor substrates.";
RL Mol. Microbiol. 77:605-617(2010).
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}.
CC -!- PTM: Probably cleaved within the membrane by Rip1 near the cytoplasmic
CC membrane interface.
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DR EMBL; AP012340; BAL68056.1; -; Genomic_DNA.
DR RefSeq; WP_003400148.1; NZ_KK339488.1.
DR AlphaFoldDB; H8F2P5; -.
DR EnsemblBacteria; BAL68056; BAL68056; ERDMAN_4292.
DR KEGG; mtn:ERDMAN_4292; -.
DR PATRIC; fig|652616.3.peg.4374; -.
DR HOGENOM; CLU_080969_0_0_11; -.
DR Proteomes; UP000007568; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
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_0000422685"
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