ID A0A0B4XKU3_9GAMM Unreviewed; 264 AA.
AC A0A0B4XKU3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=S7S_12410 {ECO:0000313|EMBL:AJD48894.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD48894.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD48894.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD48894.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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}; 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}.
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DR EMBL; CP004387; AJD48894.1; -; Genomic_DNA.
DR RefSeq; WP_008738790.1; NZ_CP004387.1.
DR AlphaFoldDB; A0A0B4XKU3; -.
DR STRING; 391936.S7S_12410; -.
DR MEROPS; S26.001; -.
DR KEGG; apac:S7S_12410; -.
DR HOGENOM; CLU_028723_1_1_6; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000006764; 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; IPR019758; Pept_S26A_signal_pept_1_CS.
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; 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|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000006764};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 42..60
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 41..240
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 70
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 264 AA; 30149 MW; D664C0959C79172F CRC64;
MEIDIGFWLT LAVFISGVIW LLDWKFKLRE RGGKAVKETV EFTNSLLPVF FVVLVIRSFV
VEPFTIPSGS MLPTLEVNDF ILVNKFAYGL RLPVTNTRIL DLGDPERGDV MVFRYPLKPA
QNFIKRVVGV PGDRISQRGG QLYINGEPLP REQIASERMG RLQETLYEET LGETRHLVRH
EAEINPFTGA LMSRSEDKDW VVGEGEYFMV GDNRNNSNDS RYWGMVPEDH IVGKAFLIWM
HWRPGLSLPS FSRNGAIDKL DDAD
//