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Database: UniProt
Entry: V6ITV0_9BACL
LinkDB: V6ITV0_9BACL
Original site: V6ITV0_9BACL 
ID   V6ITV0_9BACL            Unreviewed;       193 AA.
AC   V6ITV0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   ORFNames=P343_17200 {ECO:0000313|EMBL:EST10383.1};
OS   Sporolactobacillus laevolacticus DSM 442.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC   Sporolactobacillus.
OX   NCBI_TaxID=1395513 {ECO:0000313|EMBL:EST10383.1, ECO:0000313|Proteomes:UP000018296};
RN   [1] {ECO:0000313|EMBL:EST10383.1, ECO:0000313|Proteomes:UP000018296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 442 {ECO:0000313|EMBL:EST10383.1,
RC   ECO:0000313|Proteomes:UP000018296};
RX   PubMed=24371202;
RA   Wang H., Wang L., Ju J., Yu B., Ma Y.;
RT   "Genome Sequence of Sporolactobacillus laevolacticus DSM442, an Efficient
RT   Polymer-Grade D-Lactate Producer from Agricultural Waste Cottonseed as a
RT   Nitrogen Source.";
RL   Genome Announc. 1:e01100-13(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|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU003993};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606, 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:EST10383.1}.
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DR   EMBL; AWTC01000024; EST10383.1; -; Genomic_DNA.
DR   RefSeq; WP_023511632.1; NZ_AWTC01000024.1.
DR   AlphaFoldDB; V6ITV0; -.
DR   STRING; 1395513.P343_17200; -.
DR   PATRIC; fig|1395513.3.peg.3489; -.
DR   eggNOG; COG0681; Bacteria.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000018296; Unassembled WGS sequence.
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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR   InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
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; 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   Membrane {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018296};
KW   Transmembrane {ECO:0000256|RuleBase:RU003993};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   DOMAIN          13..179
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        84
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   193 AA;  22138 MW;  E8F9C338F29385A1 CRC64;
     MNESMSKTKR ELWSWIKAVA IAILIALLVR NFIFSNYIVR GESMMPTLQD GNRLIVNKIG
     YEIGNPHRFD IIVFHATKTD DYVKRVIGLP GDTISYNNDQ LYVNGKAVAE PYLQQYKDAL
     PKGQQLTDNF SLQSKTGKLR VPKGELWVMG DNRQNSEDSR YFGFIQEKSV VGKVAVRYWP
     FDKWAVLQIA SKN
//
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