ID J7Q858_METSZ Unreviewed; 333 AA.
AC J7Q858;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Signal peptide peptidase SppA, 36K type {ECO:0000313|EMBL:CCJ06702.1};
GN OrderedLocusNames=BN69_1251 {ECO:0000313|EMBL:CCJ06702.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ06702.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ06702.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ06702.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; HE956757; CCJ06702.1; -; Genomic_DNA.
DR AlphaFoldDB; J7Q858; -.
DR STRING; 187303.BN69_1251; -.
DR KEGG; msc:BN69_1251; -.
DR PATRIC; fig|187303.17.peg.1361; -.
DR eggNOG; COG0616; Bacteria.
DR HOGENOM; CLU_046540_0_0_5; -.
DR Proteomes; UP000005263; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 118..267
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 333 AA; 35828 MW; D9AF409FB6FB3AC1 CRC64;
MRRASLRDPW MSPPTDYFVD RRRLRRKLGW WRLAALIAIG VAGLIAVVRL GGADSADKLT
PHIARLELQG VITGDDDTID MIKKIGESSQ TKALLLEIES PGGTTTGSER LYEELRRVAE
KKPVVAVVGT VAASGAYIAA LAADTIVARG NSLIGSIGVL FQYPNVSKLL NNWGVEVETI
KSSPLKAAPN GLEPTSPQAR EAVASLVADS YAWFKGLVRE RRNLDEAELA KVADGRVFTA
RQGVPLKLVD LIGGQREAID WLVANKGIAK DTPVREWKKK SSLERLGLVG AAAGLARVAG
LESIAGFLEK SILLERSGEL DGLLAIWQHS AAN
//
