ID A0A2R8BHN0_9RHOB Unreviewed; 378 AA.
AC A0A2R8BHN0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 Name=lepB_1 {ECO:0000313|EMBL:SPH22591.1};
GN ORFNames=ASD8599_03334 {ECO:0000313|EMBL:SPH22591.1};
OS Ascidiaceihabitans donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Ascidiaceihabitans.
OX NCBI_TaxID=1510460 {ECO:0000313|EMBL:SPH22591.1, ECO:0000313|Proteomes:UP000244880};
RN [1] {ECO:0000313|EMBL:SPH22591.1, ECO:0000313|Proteomes:UP000244880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8599 {ECO:0000313|EMBL:SPH22591.1,
RC ECO:0000313|Proteomes:UP000244880};
RA Keele B.F.;
RL Submitted (MAR-2018) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; OMOR01000001; SPH22591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8BHN0; -.
DR Proteomes; UP000244880; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; IPR008523; DUF805.
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; 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; PF05656; DUF805; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:SPH22591.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000244880};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 141..354
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 164
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 220
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 378 AA; 40739 MW; 11278EA32391E03D CRC64;
MISDSRRTSG PAPHLGPVRA VIDCVRLMFT FSGRASRSAF IWPVIFALIV IVVASLVYHA
LVPATVSFGY IRFVTVTVAL PLLPLGVRRL HDMGMSGWWA LLWLVPYVGF ILTLFAAFKR
AELGTNQYDH SDPSVFGQIA VVGGFVALVG VTFAVQPFWI PGGSMKPTVV VGDYITVSTT
AYGLPCFGLC GDADRMLQRN PDRGDVVVFK HPVTGRDFIK RVIAVSGDTV ALEDGQVVVN
GAGLTQTAQG DYVEPMEMQG LGHALPRCRT VTPLGGRCAK SLLQETTSDG RRYGILDISR
TQADSMAQIT VPDGMIFVLG DNRDNSADSR MAQAAGGVGF VPVENLVGRA TRVVVSNAGF
ALWDPTGFRG ARFWTKIR
//
