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Database: UniProt
Entry: A0A418V5A6_9DEIO
LinkDB: A0A418V5A6_9DEIO
Original site: A0A418V5A6_9DEIO 
ID   A0A418V5A6_9DEIO        Unreviewed;       234 AA.
AC   A0A418V5A6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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   Name=lepB {ECO:0000313|EMBL:RJF71292.1};
GN   ORFNames=D3875_06610 {ECO:0000313|EMBL:RJF71292.1};
OS   Deinococcus cavernae.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=2320857 {ECO:0000313|EMBL:RJF71292.1, ECO:0000313|Proteomes:UP000286287};
RN   [1] {ECO:0000313|EMBL:RJF71292.1, ECO:0000313|Proteomes:UP000286287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2S05-167 {ECO:0000313|EMBL:RJF71292.1,
RC   ECO:0000313|Proteomes:UP000286287};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU003993};
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}.
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:RJF71292.1}.
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DR   EMBL; QYUJ01000014; RJF71292.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418V5A6; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000286287; 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; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:RJF71292.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286287}.
FT   DOMAIN          13..191
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          200..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   234 AA;  26087 MW;  16CE54BAB08E85C6 CRC64;
     MKRGQLTANL REWTSTLLFA LGFTQFAASA VQVDGTSMLP TLRHGEVLLL PKLEGWAHRA
     GWGQYQRGDI VVFKPPRDME AEWTNQYRGL PLPWKYRPYL VKRVVGMPGD TVQIRAGVLY
     VNGRRVDEPG VLNYWQSFCH DVASDLANTS PVRIPARQYF VMGDNRSPGG SLDSRVFGPV
     SVHDIAARAP LSVLPLLRQG QVTPPCDTQP HPEQRTQPGG ALEWSPRLLP PVGR
//
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