ID A0A372INI0_9BACT Unreviewed; 338 AA.
AC A0A372INI0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:RFU16444.1};
GN ORFNames=D0Y96_13785 {ECO:0000313|EMBL:RFU16444.1};
OS Paracidobacterium acidisoli.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Paracidobacterium.
OX NCBI_TaxID=2303751 {ECO:0000313|EMBL:RFU16444.1, ECO:0000313|Proteomes:UP000264702};
RN [1] {ECO:0000313|EMBL:RFU16444.1, ECO:0000313|Proteomes:UP000264702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G-K13 {ECO:0000313|EMBL:RFU16444.1,
RC ECO:0000313|Proteomes:UP000264702};
RA Gao Z.-H., Qiu L.-H.;
RT "Acidipila sp. 4G-K13, an acidobacterium isolated from forest soil.";
RL Submitted (AUG-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: 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:RFU16444.1}.
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DR EMBL; QVQT01000004; RFU16444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372INI0; -.
DR Proteomes; UP000264702; 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; 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; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:RFU16444.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000264702};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 106..295
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 186
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 338 AA; 38618 MW; 646BEDEDC7CC27D7 CRC64;
MAAAQRRWPG ARVQPGSWRS RKQHAGPWRS WLPLRKRMVN DAGEPMKTGL DESREAFGEG
SGLTAGANGL AQATLPPPPD GAEVRRGPSA HPHSHFHIYP GPLDTTQSLL SILVIAIFVL
TFIVQPFRIP SESMERTLLV GDFLLVNKTI FGPPGHWKWL LPYRPEERGD VVVFYFPVNP
AEHVVKRVIG VPGDRIHLRG GVVYRNGQPL NEPYVVFEPA YPDNFRDNFP IRIYTDPGVD
MHWWQQLRRT EQQGDVVVPA GQYFVMGDNR NHSRDSRYWG FVPEREVVGR PFVIYFSLRR
PSTTDVQLPP DDKLGHNKDL LTRVLNFARW GRFLRIIR
//
