ID   RSEA_ECOL6              Reviewed;         216 AA.
AC   P0AFX8; P38106;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Anti-sigma-E factor RseA;
DE   AltName: Full=Regulator of SigE;
DE   AltName: Full=Sigma-E anti-sigma factor RseA;
DE   AltName: Full=Sigma-E factor negative regulatory protein;
GN   Name=rseA; Synonyms=mclA; OrderedLocusNames=c3096;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: An anti-sigma factor for extracytoplasmic function (ECF)
CC       sigma factor sigma-E (RpoE). ECF sigma factors are held in an inactive
CC       form by an anti-sigma factor until released by regulated intramembrane
CC       proteolysis (RIP). RIP occurs when an extracytoplasmic signal triggers
CC       a concerted proteolytic cascade to transmit information and elicit
CC       cellular responses. The membrane-spanning regulatory substrate protein
CC       is first cut periplasmically (site-1 protease, S1P, DegS), then within
CC       the membrane itself (site-2 protease, S2P, RseP), while cytoplasmic
CC       proteases finish degrading the anti-sigma factor, liberating sigma-E
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts 1:1 with ECF RNA polymerase sigma-E (RpoE); this
CC       inhibits the interaction of sigma-E with the RNA polymerase catalytic
CC       core and leads to a decreased expression of sigma-E-regulated genes.
CC       Interacts with RseB with 1:1 stoichiometry. The liberated N-terminus
CC       forms a complex with SspB and RpoE (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}. Note=Following cleavage by DegS
CC       the large fragment of the protein is still in the inner membrane and
CC       retains its anti-sigma-E activity. {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal cytosolic domain interacts with sigma-E. After
CC       degradation by RseP binds to SspB, targeting RseA for degradation by
CC       the ClpX-ClpP protease (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal periplasmic domain interacts with RseB and is
CC       also the target for DegS. {ECO:0000250}.
CC   -!- PTM: Sequentially cleaved by DegS (a site-1 protease) in its
CC       periplasmic domain between Val-148 and Ser-149, then by RseP (a site-2
CC       protease) between positions Ala-108 and Cys-109. The N-terminal
CC       fragment is then degraded by primarily ClpX-ClpP in an ATP-dependent
CC       fashion. Sequential cleavage by DegS, RseP and ClpX-ClpP frees RpoE
CC       from RseA (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RseA family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN81545.1; -; Genomic_DNA.
DR   RefSeq; WP_001168459.1; NC_004431.1.
DR   AlphaFoldDB; P0AFX8; -.
DR   SMR; P0AFX8; -.
DR   STRING; 199310.c3096; -.
DR   EnsemblBacteria; AAN81545; AAN81545; c3096.
DR   GeneID; 66673539; -.
DR   KEGG; ecc:c3096; -.
DR   eggNOG; COG3073; Bacteria.
DR   HOGENOM; CLU_108851_1_0_6; -.
DR   OMA; PEWNIAE; -.
DR   BioCyc; ECOL199310:C3096-MON; -.
DR   EvolutionaryTrace; P0AFX8; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016989; F:sigma factor antagonist activity; IEA:InterPro.
DR   CDD; cd16328; RseA_N; 1.
DR   Gene3D; 1.10.10.880; -; 1.
DR   InterPro; IPR005573; Anti-sigma_E_RseA_C.
DR   InterPro; IPR005572; Anti-sigma_E_RseA_N.
DR   InterPro; IPR036147; Anti-sigma_E_RseA_N_sf.
DR   InterPro; IPR026279; RseA.
DR   Pfam; PF03873; RseA_C; 1.
DR   Pfam; PF03872; RseA_N; 1.
DR   PIRSF; PIRSF016938; RseA; 1.
DR   SUPFAM; SSF89069; SSF89069; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..216
FT                   /note="Anti-sigma-E factor RseA"
FT                   /id="PRO_0000097481"
FT   TRANSMEM        101..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          146..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            108..109
FT                   /note="Cleavage; by RseP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24321 MW;  63BD12131C611C32 CRC64;
     MQKEQLSALM DGETLDSELL NELAHNPEMQ KTWESYHLIR DSMRGDTPEV LHFDISSRVM
     AAIEEEPVRQ PATLIPEAQP APHQWQKMPF WQKVRPWAAQ LTQMGVAACV SLAVIVGVQH
     YNGQSETSQQ PETPVFNTLP MMGKASPVSL GVPSEATANN GQQQQVQEQR RRINAMLQDY
     ELQRRLHSEQ LQFEQAQTQQ AAVQVPGIQT LGTQSQ