ID F2N9F6_CORGP Unreviewed; 186 AA.
AC F2N9F6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=Corgl_0872 {ECO:0000313|EMBL:AEB06985.1};
OS Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / PW2).
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Coriobacterium.
OX NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB06985.1, ECO:0000313|Proteomes:UP000006851};
RN [1] {ECO:0000313|Proteomes:UP000006851}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2
RC {ECO:0000313|Proteomes:UP000006851};
RX PubMed=23961308; DOI=10.4056/sigs.3507020;
RA Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Chang Y.J., Land M., Hauser L., Rohde M.,
RA Pukall R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Coriobacterium glomerans type strain (PW2(T))
RT from the midgut of Pyrrhocoris apterus L. (red soldier bug).";
RL Stand. Genomic Sci. 8:15-25(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP002628; AEB06985.1; -; Genomic_DNA.
DR RefSeq; WP_013708728.1; NC_015389.1.
DR AlphaFoldDB; F2N9F6; -.
DR STRING; 700015.Corgl_0872; -.
DR MEROPS; S26.024; -.
DR KEGG; cgo:Corgl_0872; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_11; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000006851; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:AEB06985.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000006851};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 13..178
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 186 AA; 20597 MW; 01AD23FEBC141AE6 CRC64;
MASKRHSVLR SALEWITLLV AAFCLFVFTR TFVTEPFSVP TGSMEPTIKT GDQIFVQKLT
KEFGIHVKRG DIVVFRNLDL ASSHEILVKR VIATAGQTVD FKDGHVCVDG IELEEPYAKG
VSAPLPNHAP GTSISFPLTV PDGQVWLMGD NRENSSDSRF FGPVPEDDLV GSVFIRYWPL
SRFGMP
//
