GenomeNet

Database: UniProt
Entry: Q2NS12_SODGM
LinkDB: Q2NS12_SODGM
Original site: Q2NS12_SODGM 
ID   Q2NS12_SODGM            Unreviewed;       328 AA.
AC   Q2NS12;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 115.
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   Name=lepB {ECO:0000313|EMBL:CRL45974.1};
GN   OrderedLocusNames=SG1788 {ECO:0000313|EMBL:BAE75063.1};
GN   ORFNames=SGGMMB4_04173 {ECO:0000313|EMBL:CRL45974.1};
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509 {ECO:0000313|EMBL:BAE75063.1, ECO:0000313|Proteomes:UP000001932};
RN   [1] {ECO:0000313|EMBL:BAE75063.1, ECO:0000313|Proteomes:UP000001932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans {ECO:0000313|Proteomes:UP000001932}, and Morsitans
RC   {ECO:0000313|EMBL:BAE75063.1};
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
RN   [2] {ECO:0000313|EMBL:CRL45974.1, ECO:0000313|Proteomes:UP000245838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:CRL45974.1}, and morsitans
RC   {ECO:0000313|Proteomes:UP000245838};
RA   Goodhead I.;
RL   Submitted (MAY-2015) 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|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   ---------------------------------------------------------------------------
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; AP008232; BAE75063.1; -; Genomic_DNA.
DR   EMBL; LN854557; CRL45974.1; -; Genomic_DNA.
DR   RefSeq; WP_011411612.1; NZ_LN854557.1.
DR   STRING; 343509.SG1788; -.
DR   MEROPS; S26.001; -.
DR   KEGG; sgl:SG1788; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_1_6; -.
DR   OrthoDB; 9815782at2; -.
DR   BioCyc; SGLO343509:SGP1_RS16220-MONOMER; -.
DR   Proteomes; UP000001932; Chromosome.
DR   Proteomes; UP000245838; Chromosome sggmmb4_Chromosome.
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          64..306
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   328 AA;  36181 MW;  59001EAA4CACCEA5 CRC64;
     MANMFALIMA IATLITGILW CLERFKLAPA RRRLGQQPGQ QRPEAVGGTP GNDVAVKVSH
     KPGWIETCAS IFPVLLLVFV VRSFIFEPFQ IPSGSMMPTL LVGDFILVEK FAYGIKDPIT
     HTTLIETGHP KRGDVVVFKF PLDPKLDYIK RVVGLPGDRV SYDPVNKRLT VQPGCASGQD
     CATAVPITYS ERAPSDFEQT FNSTGDGEAS SGFLQVPPDR EVDGAIRLAQ RKESLGGVVH
     NILMVPGKQD QLGIYYQQQG SLLAEWVVPQ GEYFMMGDNR DNSADSRFWG FVPERNLVGK
     ATAIWMSFEK QEGQWPTGVR LSRIGGIH
//
DBGET integrated database retrieval system