RSKA_MYCBP
ID RSKA_MYCBP Reviewed; 232 AA.
AC A1KFR6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Dysfunctional anti-sigma-K factor RskA;
DE AltName: Full=Regulator of SigK;
DE AltName: Full=Sigma-K anti-sigma factor RskA;
GN Name=rskA; OrderedLocusNames=BCG_0483c;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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). However, in M.bovis this protein is probably dysfunctional, due
CC to at least 1 of the 2 naturally occurring polymorphisms in its gene,
CC when compared to M.tuberculosis. This leads to an increased expression
CC of SigK-regulated genes, such as mpb70 and mpb83. RIP occurs when an
CC extracytoplasmic signal triggers a concerted proteolytic cascade to
CC transmit information and elicit cellular responses. The membrane-
CC spanning regulatory substrate protein is first cut extracytoplasmically
CC (site-1 protease, S1P), then within the membrane itself (site-2
CC protease, S2P, Rip1), while cytoplasmic proteases finish degrading the
CC regulatory protein, liberating the sigma factor (By similarity).
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM408590; CAL70468.1; -; Genomic_DNA.
DR RefSeq; WP_010950404.1; NC_008769.1.
DR AlphaFoldDB; A1KFR6; -.
DR SMR; A1KFR6; -.
DR KEGG; mbb:BCG_0483c; -.
DR HOGENOM; CLU_075802_1_1_11; -.
DR OMA; VYQMWLI; -.
DR Proteomes; UP000001472; 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="Dysfunctional anti-sigma-K factor RskA"
FT /id="PRO_0000313831"
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; 24013 MW; 84F732430EE3C7EA CRC64;
MTEHTDFELL ELATPYALNA VSDDERADID RRVAAAPSPV AAAFNDEVRA VRETMAVVSA
ATTAEPPAHL RTAILDATKP EVRRQSRWRT AAFASAAAIA VGLGAFDLGV LTRPSPPPTV
AEQVLTAPDV RTVSRPLGAG TATVVFSRDR NTGLLVMNNV APPSRGTVYQ MWLLGGAKGP
RSAETMGTAA VTPSTTATLT DLGASTALAF TVEPGTGSPQ PTGTILAELP LG