ID A0A1R0IQJ7_SULTH Unreviewed; 172 AA.
AC A0A1R0IQJ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN Name=lepB {ECO:0000313|EMBL:PSR29874.1};
GN ORFNames=C7B47_00770 {ECO:0000313|EMBL:PSR29874.1};
OS Sulfobacillus thermosulfidooxidans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales;
OC Clostridiales Family XVII. Incertae Sedis; Sulfobacillus.
OX NCBI_TaxID=28034 {ECO:0000313|EMBL:PSR29874.1, ECO:0000313|Proteomes:UP000242705};
RN [1] {ECO:0000313|EMBL:PSR29874.1, ECO:0000313|Proteomes:UP000242705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMDSBA5 {ECO:0000313|EMBL:PSR29874.1};
RX PubMed=25511286; DOI=10.1186/1471-2164-15-1107;
RA Justice N.B., Norman A., Brown C.T., Singh A., Thomas B.C., Banfield J.F.;
RT "Comparison of environmental and isolate Sulfobacillus genomes reveals
RT diverse carbon, sulfur, nitrogen, and hydrogen metabolisms.";
RL BMC Genomics 15:1107-1107(2014).
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: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606,
CC ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, 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:PSR29874.1}.
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DR EMBL; PXYX01000001; PSR29874.1; -; Genomic_DNA.
DR RefSeq; WP_020374725.1; NZ_MDZF01000020.1.
DR AlphaFoldDB; A0A1R0IQJ7; -.
DR Proteomes; UP000242705; 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; 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 Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 10..163
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 172 AA; 19961 MW; 02322496371787AC CRC64;
MTNQRRRGYL EFIETVILAV VLAFLIRTFV FESYQVEGIS MLPTLHTGER VLVNKLIYDF
ETPKTGQIIV FRSPVIKSQD WIKRVIGVPG DTISVKNNVV YINGKRYHEP FLKYRGSMNV
PPTKVPPGYL WVEGDNRPKS FDSRYFGLLP MKNVKGEAFV VWWPLSDFHL LH
//
