ID D7IHI9_9BACE Unreviewed; 312 AA.
AC D7IHI9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN ORFNames=HMPREF9007_03855 {ECO:0000313|EMBL:EFI03110.1};
OS Bacteroides sp. 1_1_14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI03110.1, ECO:0000313|Proteomes:UP000003951};
RN [1] {ECO:0000313|EMBL:EFI03110.1, ECO:0000313|Proteomes:UP000003951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_14 {ECO:0000313|EMBL:EFI03110.1,
RC ECO:0000313|Proteomes:UP000003951};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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; GG774709; EFI03110.1; -; Genomic_DNA.
DR RefSeq; WP_008762920.1; NZ_GG774709.1.
DR AlphaFoldDB; D7IHI9; -.
DR HOGENOM; CLU_028723_1_0_10; -.
DR Proteomes; UP000003951; 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; 2.
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; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042}.
FT DOMAIN 6..113
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 254..290
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 312 AA; 35822 MW; F721A710C0A82BC7 CRC64;
MNIRKLKWIF AFAGAIAVVL LLRGFAFTSC LIPSTGMENS LFQGERILVN KWSYGLRLPL
MSLFSYHRWC ERSVRKQDVV VFNNPAAIGQ PTIDRREIYI SRCIGTPGDT LLVDSLFSVS
SPEAQLNPDK KRLYTYPAAK EQLITSLMQT LSITNDGLMG SNDSTHVRSF SRYEYYLLEQ
AISDQNWIQP LTEKSEKELK PLIVPGKGKA LRVYPWNITL LRNTLVMHEG KQAEIKNDTL
YIDGKPTQHC FFTKDYYWMA SNNSVNLSDS RLFGFVPQDH IIGKASLIWF SKEKGTGIFD
GYRWNRFFQS VK
//
