ID   RSKA_MYCVP              Reviewed;         238 AA.
AC   A1TEV1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Mvan_4928;
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1;
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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; CP000511; ABM15701.1; -; Genomic_DNA.
DR   RefSeq; WP_011782073.1; NC_008726.1.
DR   AlphaFoldDB; A1TEV1; -.
DR   SMR; A1TEV1; -.
DR   STRING; 350058.Mvan_4928; -.
DR   EnsemblBacteria; ABM15701; ABM15701; Mvan_4928.
DR   KEGG; mva:Mvan_4928; -.
DR   eggNOG; COG5343; Bacteria.
DR   HOGENOM; CLU_075802_1_1_11; -.
DR   OMA; VYQMWLI; -.
DR   OrthoDB; 1740922at2; -.
DR   Proteomes; UP000009159; 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; Reference proteome; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN           1..238
FT                   /note="Anti-sigma-K factor RskA"
FT                   /id="PRO_0000313838"
FT   TOPO_DOM        1..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   238 AA;  24422 MW;  DDC5E0326888A33D CRC64;
     MTSPQNDLLS LATPYALHAL SHAEAADIDR ALNDAPPGVA DAFLAEVRAV RETMAALASA
     TAVEPPARMR DAVLRQIAED PVRTLPVRSS SRRRAAAVLS AAAAVVIGLG TLAVGYALRP
     APTPSTAEQV FAAPDVRTIS GEIPGGGTAT VVFSREQNSG VLVMNNVPPP QPGTVYQMWL
     VDADGSHSAG TMDAEAVAPS TTAVLPDLGS SRALAFTVEP PGGSTRPTTP VFAELPLT