SP2G_CLOAB
ID SP2G_CLOAB Reviewed; 266 AA.
AC Q45832; Q45803;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable sporulation sigma-E factor-processing peptidase;
DE EC=3.4.23.-;
DE AltName: Full=Membrane-associated aspartic protease;
DE AltName: Full=Stage II sporulation protein GA;
GN Name=spoIIGA; OrderedLocusNames=CA_C1694;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=7961408; DOI=10.1128/jb.176.21.6572-6582.1994;
RA Sauer U., Treuner A., Buchholz M., Santangelo J.D., Durre P.;
RT "Sporulation and primary sigma factor homologous genes in Clostridium
RT acetobutylicum.";
RL J. Bacteriol. 176:6572-6582(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=7883192; DOI=10.1016/0378-1119(94)00818-d;
RA Wong J., Sass C., Bennett G.N.;
RT "Sequence and arrangement of genes encoding sigma factors in Clostridium
RT acetobutylicum ATCC 824.";
RL Gene 153:89-92(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- FUNCTION: Probable aspartic protease that is responsible for the
CC proteolytic cleavage of the RNA polymerase sigma E factor
CC (SigE/spoIIGB) to yield the active peptide in the mother cell during
CC sporulation. Responds to a signal from the forespore that is triggered
CC by the extracellular signal protein SpoIIR (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase U4 family. {ECO:0000305}.
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DR EMBL; Z23079; CAA80616.1; -; Genomic_DNA.
DR EMBL; U07420; AAC43308.1; -; Genomic_DNA.
DR EMBL; AE001437; AAK79660.1; -; Genomic_DNA.
DR PIR; A97109; A97109.
DR PIR; I40626; I40626.
DR RefSeq; NP_348320.1; NC_003030.1.
DR RefSeq; WP_010965001.1; NC_003030.1.
DR AlphaFoldDB; Q45832; -.
DR STRING; 272562.CA_C1694; -.
DR EnsemblBacteria; AAK79660; AAK79660; CA_C1694.
DR GeneID; 44998189; -.
DR KEGG; cac:CA_C1694; -.
DR PATRIC; fig|272562.8.peg.1897; -.
DR eggNOG; ENOG50301AF; Bacteria.
DR HOGENOM; CLU_059158_0_0_9; -.
DR OMA; IYLDVIW; -.
DR OrthoDB; 1492550at2; -.
DR Proteomes; UP000000814; 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:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0030436; P:asexual sporulation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR InterPro; IPR005081; SpoIIGA.
DR Pfam; PF03419; Peptidase_U4; 1.
DR PIRSF; PIRSF018571; SpoIIGA; 1.
DR TIGRFAMs; TIGR02854; spore_II_GA; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..266
FT /note="Probable sporulation sigma-E factor-processing
FT peptidase"
FT /id="PRO_0000079181"
FT TRANSMEM 36..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 174
FT /evidence="ECO:0000250"
FT CONFLICT 249
FT /note="N -> Y (in Ref. 2; AAC43308)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 266 AA; 30609 MW; 5E73DF9E991F4348 CRC64;
MVIYLDVLIF ENSIVNTFLL YITAQTLRIK VKMRYLILAG IFGGLYVIVL VIPTLKIFSS
LIFKIIAAFL MIIICFRKKS LRFNIKALAV LIMYSMVTAG LCFFIELNNT RGSYFNAFIG
NVSYKWILIA IMIIYMFVNR IIWFINDRKL TQSLIYEIEI CFKDNSKFIN AFLDTGNELR
EPITNLPVIV VEKDMVSGIK WDDCPKFYVP FRLFNGKAGN LEAFKPSYVK IYIGDKVEVR
NAIIALIDNK LSSLNDYNAL LSRGSI