ID RSKA_MYCSK Reviewed; 243 AA.
AC A1ULE2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
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=Mkms_4459;
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL93650.1; -; Genomic_DNA.
DR AlphaFoldDB; A1ULE2; -.
DR SMR; A1ULE2; -.
DR STRING; 189918.Mkms_4459; -.
DR KEGG; mkm:Mkms_4459; -.
DR HOGENOM; CLU_075802_1_1_11; -.
DR OrthoDB; 153510at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.10.1320; Anti-sigma factor, zinc-finger domain; 1.
DR InterPro; IPR018764; Anti-sigma_K_RskA.
DR InterPro; IPR041916; Anti_sigma_zinc_sf.
DR PANTHER; PTHR37461; ANTI-SIGMA-K FACTOR RSKA; 1.
DR PANTHER; PTHR37461:SF1; ANTI-SIGMA-K FACTOR RSKA; 1.
DR Pfam; PF10099; RskA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..243
FT /note="Anti-sigma-K factor RskA"
FT /id="PRO_0000313833"
FT TOPO_DOM 1..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 223..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 25147 MW; 8A266BE514208FE8 CRC64;
MTEPNNTDLL DLATPYALHA VSIDERFEID RWLATAPPEV ADAFTDEVRS VQETMAVLSA
ATATEPPAHL RDNVLAMVAD DPVRDLGSAR RRRGGESRWR TAVLAAAAVA VVGLGALGVG
LALRPAVSPT TADQVFAAPD VQTVSGPIPG GGTATVVFSK ERDAGVLVMN DVAPPKPGTV
YQMWLVGSDG PHSAGTMDDK AISPSTTAVL SDIGTSQALA FTVEPPGGSQ RPTSPAFAEL
PLT
//
