ID E3D7K7_GARV3 Unreviewed; 194 AA.
AC E3D7K7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:ADP39299.1};
GN OrderedLocusNames=HMPREF0421_21217 {ECO:0000313|EMBL:ADP39299.1};
OS Gardnerella vaginalis (strain ATCC 14019 / 317).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=525284 {ECO:0000313|EMBL:ADP39299.1, ECO:0000313|Proteomes:UP000001453};
RN [1] {ECO:0000313|EMBL:ADP39299.1, ECO:0000313|Proteomes:UP000001453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14019 / 317 {ECO:0000313|Proteomes:UP000001453};
RX PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA Wilson B.A.;
RT "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT differences in metabolic and virulence potential.";
RL PLoS ONE 5:E12411-E12411(2010).
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|ARBA:ARBA00000677,
CC 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; CP002104; ADP39299.1; -; Genomic_DNA.
DR RefSeq; YP_003986322.1; NC_014644.1.
DR AlphaFoldDB; E3D7K7; -.
DR MEROPS; S26.025; -.
DR KEGG; gvg:HMPREF0421_21217; -.
DR PATRIC; fig|525284.18.peg.1199; -.
DR HOGENOM; CLU_028723_0_2_11; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000001453; Chromosome.
DR GO; GO:0005886; C:plasma 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; IPR019758; Pept_S26A_signal_pept_1_CS.
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.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:ADP39299.1};
KW Protease {ECO:0000256|RuleBase:RU362042}.
FT DOMAIN 3..169
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 23
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 194 AA; 21284 MW; FA9A6A0EC992B0CA CRC64;
MPILVVIFLR VFILGVYFIP SGSMLDTIHI GDYVVTSKLT PRLFPLNRGD IVVFEDPANW
LQGENSRGGI VSGKDLIKRL IGLPGDTVEC KGDGDPILVN GVPVLESAYI KPGVSPSSFP
FKVKVKPGHV FVLGDNRANS ADSRYHKNDG DDGLVPISKV EGVAFMRFWP LNRMGIFENH
SDAFDDVRNK SDAK
//