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Database: UniProt
Entry: H5SIN9_9BACT
LinkDB: H5SIN9_9BACT
Original site: H5SIN9_9BACT 
ID   H5SIN9_9BACT            Unreviewed;       313 AA.
AC   H5SIN9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   ORFNames=HGMM_F33H03C34 {ECO:0000313|EMBL:BAL56025.1};
OS   uncultured Bacteroidetes bacterium.
OC   Bacteria; Bacteroidota; environmental samples.
OX   NCBI_TaxID=152509 {ECO:0000313|EMBL:BAL56025.1};
RN   [1] {ECO:0000313|EMBL:BAL56025.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA   Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA   Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT   "Genetic and functional properties of uncultivated thermophilic
RT   crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT   genome fragments.";
RL   Environ. Microbiol. 7:1967-1984(2005).
RN   [2] {ECO:0000313|EMBL:BAL56025.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA   Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT   "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT   Pathway Dominates a Subsurface Ecosystem.";
RL   PLoS ONE 7:e30559-e30559(2012).
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: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; AP011735; BAL56025.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5SIN9; -.
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; 2.
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; 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; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042}.
FT   DOMAIN          38..282
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   313 AA;  36573 MW;  EA20F76D2849096D CRC64;
     MFKELWQQVV RFYQWRKERK AERKRRYRQM TFPQKVVAWV RSLAGAFIVV VILNGLAVAA
     FEVPTGSMEN TVMAGENLFV NKFIFGPSTP QIIPLFNIPL PYYKLPPLRD PQRGDVIVFI
     YPGDRDEVKP KEFMYYLKRC IAVAGDTLLI RNDSVFVNGQ FMPFPKHAKF LPTPDDPSRI
     FPPGKGWTRS NYGPLRIPKK GDIIHLDADN FIEWEIFIRR EGHDVDFRLG EVYIDGKPTT
     TYTVERDYVF GMGDNRNNSL DSRYWGFIPK ENVVGTPLFV YWSWEKTDLN GNPLPLLKRL
     TRIRWSRLGT IVR
//
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