ID B3EPG9_CHLPB Unreviewed; 275 AA.
AC B3EPG9;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN OrderedLocusNames=Cphamn1_0902 {ECO:0000313|EMBL:ACE03847.1};
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678 {ECO:0000313|EMBL:ACE03847.1};
RN [1] {ECO:0000313|EMBL:ACE03847.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1 {ECO:0000313|EMBL:ACE03847.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) 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|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; CP001101; ACE03847.1; -; Genomic_DNA.
DR AlphaFoldDB; B3EPG9; -.
DR STRING; 331678.Cphamn1_0902; -.
DR KEGG; cpb:Cphamn1_0902; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR OrthoDB; 9802919at2; -.
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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:ACE03847.1};
KW Protease {ECO:0000256|RuleBase:RU362042}.
FT DOMAIN 14..247
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 44
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 275 AA; 31097 MW; B1A2A7DA440755A4 CRC64;
MAKGTGKTGK QHSKEWFEAL LIALLFATVI RVFVVESYRI PTGSMERTLL AGDFLFVNKF
VYGAKVPFTD IRLPQVDSVE RGDIIVFKFP KDRSLNYIKR CIAVSGDTLE IKDRTVLING
QATALPEHAQ FLAGSMPAGY PDQQIFPRYA GFNKDNYGPL RIPRKGDVVS LNEDSYYLYA
ALIREEGHTI AVPGGRILVD GKPADTYTIE QNYYFALGDN RDNSLDSRFW GFLSERDVVG
QALMVYWSWD PNISFSDPVE KVSSIRWQRT GMMVH
//
