ID A0A0F4NRK2_9VIBR Unreviewed; 298 AA.
AC A0A0F4NRK2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=TW81_00305 {ECO:0000313|EMBL:KJY85463.1};
OS Vibrio galatheae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=579748 {ECO:0000313|EMBL:KJY85463.1, ECO:0000313|Proteomes:UP000033673};
RN [1] {ECO:0000313|EMBL:KJY85463.1, ECO:0000313|Proteomes:UP000033673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2757 {ECO:0000313|EMBL:KJY85463.1,
RC ECO:0000313|Proteomes:UP000033673};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJY85463.1}.
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DR EMBL; JXXV01000002; KJY85463.1; -; Genomic_DNA.
DR RefSeq; WP_045953733.1; NZ_JXXV01000002.1.
DR AlphaFoldDB; A0A0F4NRK2; -.
DR STRING; 579748.TW81_00305; -.
DR PATRIC; fig|579748.3.peg.62; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000033673; 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 Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000033673};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 59..268
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 90
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 298 AA; 33505 MW; 28E5148CFB5EF6EB CRC64;
MANTFALILV IVTFVTGVVW VLEKLVFAKK RQAKLAEVEA QTNGIDAALL AKVKTQPWWI
ENSVSIFPVI AAVLVLRSFI YEPFQIPSGS MMPTLLVGDF ILVEKYAYGL KDPVWRTQLV
ETGKPERGDI VVFKYPPQPS IDYIKRVVGM PGDTVRYNSK KEICIQSQGD SSCQSVKLSN
VEESPFIQNG IPLIQLDEKL GQVDHQILVN PLRRDRVELY QPRNGVNEWV VPEGQYFVMG
DNRDNSADSR YWGFVPEANL VGKAVGIWIS FEFERSADSV LPSWIPTGVR FNRIGGIN
//