ID   RSKA_MYCTA              Reviewed;         232 AA.
AC   A5TZH0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Anti-sigma-K factor RskA;
DE   AltName: Full=Regulator of SigK;
DE   AltName: Full=Sigma-K anti-sigma factor RskA;
GN   Name=rskA; OrderedLocusNames=MRA_0449;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC       sigma factor SigK. 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The cytosolic domain interacts with sigma factor SigK.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anti-sigma-K factor family. {ECO:0000305}.
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DR   EMBL; CP000611; ABQ72170.1; -; Genomic_DNA.
DR   RefSeq; WP_003898455.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5TZH0; -.
DR   SMR; A5TZH0; -.
DR   STRING; 419947.MRA_0449; -.
DR   EnsemblBacteria; ABQ72170; ABQ72170; MRA_0449.
DR   KEGG; mra:MRA_0449; -.
DR   eggNOG; COG5343; Bacteria.
DR   HOGENOM; CLU_075802_1_1_11; -.
DR   OMA; VYQMWLI; -.
DR   OrthoDB; 1740922at2; -.
DR   Proteomes; UP000001988; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.10.10.1320; -; 1.
DR   InterPro; IPR018764; Anti-sigma_K_RskA.
DR   InterPro; IPR041916; Anti_sigma_zinc_sf.
DR   Pfam; PF10099; RskA; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transcription; Transcription regulation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..232
FT                   /note="Anti-sigma-K factor RskA"
FT                   /id="PRO_0000313836"
FT   TOPO_DOM        1..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..232
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   232 AA;  23883 MW;  877A84993EE217E9 CRC64;
     MTEHTDFELL ELATPYALNA VSDDERADID RRVAAAPSPV AAAFNDEVRA VRETMAVVSA
     ATTAEPPAHL RTAILDATKP EVRRQSRWRT AAFASAAAIA VGLGAFGLGV LTRPSPPPTV
     AEQVLTAPDV RTVSRPLGAG TATVVFSRDR NTGLLVMNNV APPSRGTVYQ MWLLGGAKGP
     RSAGTMGTAA VTPSTTATLT DLGASTALAF TVEPGTGSPQ PTGTILAELP LG