RSEA_HAEIN
ID RSEA_HAEIN Reviewed; 195 AA.
AC P44791;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=HI_0629;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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-147 and Ser-148, then by RseP (a site-2
CC protease). The N-terminal fragment is then degraded by primarily ClpX-
CC ClpP in an ATP-dependent fashion. Sequential cleavage by DegS, RseP and
CC ClpX-ClpP frees RpoE from RseA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RseA family. {ECO:0000305}.
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DR EMBL; L42023; AAC22289.1; -; Genomic_DNA.
DR PIR; G64082; G64082.
DR RefSeq; NP_438789.1; NC_000907.1.
DR RefSeq; WP_005651258.1; NC_000907.1.
DR AlphaFoldDB; P44791; -.
DR SMR; P44791; -.
DR STRING; 71421.HI_0629; -.
DR EnsemblBacteria; AAC22289; AAC22289; HI_0629.
DR KEGG; hin:HI_0629; -.
DR PATRIC; fig|71421.8.peg.655; -.
DR eggNOG; COG3073; Bacteria.
DR HOGENOM; CLU_108851_0_0_6; -.
DR OMA; PEWNIAE; -.
DR PhylomeDB; P44791; -.
DR BioCyc; HINF71421:G1GJ1-656-MON; -.
DR Proteomes; UP000000579; 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; IBA:GO_Central.
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; Coiled coil; Membrane;
KW Reference proteome; Signal-anchor; Transcription; Transcription regulation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..195
FT /note="Anti-sigma-E factor RseA"
FT /id="PRO_0000097482"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..117
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..195
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT COILED 160..181
FT /evidence="ECO:0000255"
FT SITE 148..149
FT /note="Cleavage; by DegS"
FT /evidence="ECO:0000250"
SQ SEQUENCE 195 AA; 21733 MW; 9BA4C6AA8F91CA0F CRC64;
MQKEQLSAYM DGEQVETDLI DALLRDEELQ ASWHSFHTVR SVMRKESAVF LGADFTAKMA
DLIELEDVKK VDVIAVSQPE PEDAHNSVFM QKLKAFFAPM TQVAVAAGVC LVAVLGVQSF
NNKNDASNLP ETPVLQTLPF NNAVQEVSYN APSKDTLTSD QLEKKSRRIG AMLQNYELQR
RMHSDALDVS SSQVR
