ID Q1Z4A7_9GAMM Unreviewed; 299 AA.
AC Q1Z4A7;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 ORFNames=P3TCK_24906 {ECO:0000313|EMBL:EAS43442.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS43442.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS43442.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS43442.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-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:RU003993};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Multi-
CC pass 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:EAS43442.1}.
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DR EMBL; AAPH01000011; EAS43442.1; -; Genomic_DNA.
DR RefSeq; WP_006232568.1; NZ_CH724136.1.
DR AlphaFoldDB; Q1Z4A7; -.
DR MEROPS; S26.001; -.
DR HOGENOM; CLU_028723_1_1_6; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000003789; 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; IPR019756; Pept_S26A_signal_pept_1_Ser-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; 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 60..269
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 91
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 146
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 299 AA; 33837 MW; A7FFD6B1CBC11AE8 CRC64;
MANTFSLILV LATLFTGLIW ALDRFVWAPK RQLKIDAAAA NAGDQVDVKT LETVAPQPSW
IESTSSMFPV IALIMVFRSF IYEPFQIPSG SMMPTLLIGD FILVEKFAYG LRDPVFRHKL
IETSEPERGD VVVFKYPPQP NIDYIKRVVG MPGDTVRYSA DKQICIAPKG TTDCKVVPLS
NMTDSEFTQN MTRLVRFNEK LGDVDHQILV NPLKRDRTLA YQPRPGITEW VVPEGEYFMM
GDNRDNSADS RYWGFVPEAN LVGKAVAIWI SFEFERSTDS VLPSWIPTDV RFNRIGSIN
//
