ID V4JKQ4_9GAMM Unreviewed; 288 AA.
AC V4JKQ4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=N838_06120 {ECO:0000313|EMBL:ESQ16331.1};
OS Thiohalocapsa sp. PB-PSB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ16331.1, ECO:0000313|Proteomes:UP000017935};
RN [1] {ECO:0000313|EMBL:ESQ16331.1, ECO:0000313|Proteomes:UP000017935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA Orphan V.J.;
RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT consortia of the Sippewissett salt marsh.";
RL Submitted (AUG-2013) 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:ESQ16331.1}.
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DR EMBL; AVFR01000214; ESQ16331.1; -; Genomic_DNA.
DR AlphaFoldDB; V4JKQ4; -.
DR PATRIC; fig|1385625.5.peg.1607; -.
DR Proteomes; UP000017935; 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:UP000017935};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 63..267
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 288 AA; 32119 MW; 154DF98612FD1565 CRC64;
MNFDFPTFLV AATGLTGGIW LIDALLFAPK RRRLAEQTAS AEGVSNVAQP TTAPPAYKEP
LLVEYARSFF PVILIVLLLR SFIVEPFRIP SGSMMPTLLV GDFILVNKFS YGLRWPVLNS
KFLALGEPEP GDVVVFRFPQ NESIDYIKRV VGVPGDQIWY HNKTLYVNRE PVHQIQLPPY
VGEGAGKGHT GLRRAVEELD GVEHDLLINP RAPDLPVGCN QLASGPIRVP KDAYFVMGDN
RDNSNDSRCW GFVPEGNLVG KAFMIWMNWD GERDGFPIAF NRLGNLIH
//
