ID Q1IZF9_DEIGD Unreviewed; 259 AA.
AC Q1IZF9;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
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 OrderedLocusNames=Dgeo_1076 {ECO:0000313|EMBL:ABF45375.1};
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795 {ECO:0000313|EMBL:ABF45375.1, ECO:0000313|Proteomes:UP000002431};
RN [1] {ECO:0000313|Proteomes:UP000002431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a {ECO:0000313|Proteomes:UP000002431};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) 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: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; CP000359; ABF45375.1; -; Genomic_DNA.
DR RefSeq; WP_011530212.1; NC_008025.1.
DR AlphaFoldDB; Q1IZF9; -.
DR STRING; 319795.Dgeo_1076; -.
DR KEGG; dge:Dgeo_1076; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_0; -.
DR Proteomes; UP000002431; 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; 2.10.109.10; 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; 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; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000002431}.
FT DOMAIN 18..213
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 108
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 259 AA; 28836 MW; B8E8856019E9990B CRC64;
MTRLNKPAPG PLGKLWKEVL EPIVFAVVIT QFVATLVGVD GVSMMPNLRD HERVFVPKYE
TWLHKAGVGD FHRGDILIFK PPREAAAQAP NLTKSAFGLW TYRPFLIKRL IGLPGDRVRV
EGGQVYVNGV RLDQSWTTDY WREQGCWDTQ SDLANHATSS AAGILPDQPE ITVPPGHYFV
MGDNRTAGGS EDSRLFGPVA KRDIAGRAVA VIWPIMRKAN ARYDCSTGRV AEFSGPNVLN
WRLLKRPEAF DTLKTQLAK
//
