ID A5PBP5_9SPHN Unreviewed; 293 AA.
AC A5PBP5;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=ED21_24721 {ECO:0000313|EMBL:EDL48993.1};
OS Erythrobacter sp. SD-21.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL48993.1, ECO:0000313|Proteomes:UP000005498};
RN [1] {ECO:0000313|EMBL:EDL48993.1, ECO:0000313|Proteomes:UP000005498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL48993.1,
RC ECO:0000313|Proteomes:UP000005498};
RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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}.
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:EDL48993.1}.
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DR EMBL; ABCG01000004; EDL48993.1; -; Genomic_DNA.
DR RefSeq; WP_006833572.1; NZ_ABCG01000004.1.
DR AlphaFoldDB; A5PBP5; -.
DR STRING; 161528.ED21_24721; -.
DR MEROPS; S26.001; -.
DR eggNOG; COG0681; Bacteria.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000005498; 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; IPR019758; Pept_S26A_signal_pept_1_CS.
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.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000005498};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 32..255
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 57
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 118
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 293 AA; 32567 MW; 3A30C7BAFA707372 CRC64;
MSADTAAVTK PDHTEKKKKD DKKVDWLAEI RGLFLMLLAV FAFHSFIAKP FYIPSESMLP
NLLVGDRLVV SKYPYGWNWS SVSFHLAPRG DWRVAPATPE YGDIVIPVHP ERDEDYIKRV
VALPGDRIAV RDGQIILNGA AIAQEAEPPL DLPVDANSDC TGFYDPTFLV TGEDGSQVCR
VPVYRETLPN GATYLIIDHT SQELDDFPEM TIPERHVFVM GDNRDHSSDS RAFGMRGLMG
PVPLENIGGR AEFITFSLDG TTSLNPVSWF TSLREGRAWT TLRPAIATGK SEE
//
