RSKA_MYCTU
ID RSKA_MYCTU Reviewed; 232 AA.
AC P9WGX5; L0T3K9; O53729; Q7D9T4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
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=Rv0444c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN ANTI-SIGMA-K FACTOR.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17064366; DOI=10.1111/j.1365-2958.2006.05455.x;
RA Said-Salim B., Mostowy S., Kristof A.S., Behr M.A.;
RT "Mutations in Mycobacterium tuberculosis Rv0444c, the gene encoding anti-
RT sigK, explain high level expression of MPB70 and MPB83 in Mycobacterium
RT bovis.";
RL Mol. Microbiol. 62:1251-1263(2006).
RN [3]
RP INTERACTION WITH SIGK.
RX PubMed=20600947; DOI=10.1016/j.pep.2010.06.018;
RA Thakur K.G., Jaiswal R.K., Shukla J.K., Praveena T., Gopal B.;
RT "Over-expression and purification strategies for recombinant multi-protein
RT oligomers: a case study of Mycobacterium tuberculosis sigma/anti-sigma
RT factor protein complexes.";
RL Protein Expr. Purif. 74:223-230(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-80 IN COMPLEX WITH SIGK, AND
RP SUBUNIT.
RA Shukla J.K., Gopal B.;
RT "Structure of extra-cytoplasmic function (ECF) sigma factor SigK in complex
RT with its negative regulator RskA from Mycobacterium tuberculosis.";
RL Submitted (JAN-2013) to the PDB data bank.
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. {ECO:0000269|PubMed:17064366}.
CC -!- SUBUNIT: Interacts with ECF RNA polymerase sigma factor SigK; this
CC inhibits the interaction of SigK with the RNA polymerase catalytic core
CC and leads to a decreased expression of SigK-regulated genes, such as
CC mpt70 and mpt83. {ECO:0000269|PubMed:20600947, ECO:0000269|Ref.5}.
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 -!- SIMILARITY: Belongs to the anti-sigma-K factor family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43175.1; -; Genomic_DNA.
DR PIR; E70830; E70830.
DR RefSeq; NP_214958.1; NC_000962.3.
DR RefSeq; WP_003898455.1; NZ_NVQJ01000002.1.
DR PDB; 4NQW; X-ray; 2.40 A; B=1-80.
DR PDBsum; 4NQW; -.
DR AlphaFoldDB; P9WGX5; -.
DR SMR; P9WGX5; -.
DR STRING; 83332.Rv0444c; -.
DR iPTMnet; P9WGX5; -.
DR PaxDb; P9WGX5; -.
DR GeneID; 886346; -.
DR KEGG; mtu:Rv0444c; -.
DR TubercuList; Rv0444c; -.
DR eggNOG; COG5343; Bacteria.
DR OMA; VYQMWLI; -.
DR PhylomeDB; P9WGX5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016989; F:sigma factor antagonist activity; IDA:MTBBASE.
DR GO; GO:0006417; P:regulation of translation; IDA:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Membrane; Reference proteome;
KW Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..232
FT /note="Anti-sigma-K factor RskA"
FT /id="PRO_0000313835"
FT TOPO_DOM 2..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"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT HELIX 9..12
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 13..17
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 23..35
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 38..58
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:4NQW"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:4NQW"
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
