ID G5LMS7_SALET Unreviewed; 350 AA.
AC G5LMS7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN ORFNames=LTSEALA_1867 {ECO:0000313|EMBL:EHC40903.1};
OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC40903.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC40903.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC40903.1,
RC ECO:0000313|Proteomes:UP000004642};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:RU003993};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362042}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC40903.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFCJ01000806; EHC40903.1; -; Genomic_DNA.
DR AlphaFoldDB; G5LMS7; -.
DR MEROPS; S26.001; -.
DR PATRIC; fig|913241.3.peg.1432; -.
DR Proteomes; UP000004642; Unassembled WGS sequence.
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; 2.170.230.10; -; 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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR019766; Sign_pep_all-beta_subdom.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
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; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993}.
FT DOMAIN 74..316
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 160
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 350 AA; 38821 MW; 42607A5D4B8575AC CRC64;
MANMFALILV IATLVTGILW CVDKFVFAPK RRVDKFVFAP NAPKRRARQA AAQTASGDAL
DNATLNKVAP KPGWLETGAS VFPVLAIVLI VRSFLYEPFQ IPSGSMMPTL LIGDFILVEK
FAYGIKDPIY QKTLIETGHP KRGDIVVFKY PEDPKLDYIK RAVGLPGDKI TYDPVAKEVT
IQPGCSSGQA CENALPVTYS NVEPSDFVQT FARRNGGEAT SGFFEVPLNE TKENGIRLTE
RKETLGDVTH RILMVPIAQD QLGMYYQQPG QPLATWVVPP GQYFMMGDNR DNSADSRYWG
FVPEANLVGK AVAIWMSFDK QEGEWPTGVR RRKGSGRQAY VRLSRIGGIH
//
