ID A0A251XCC8_9GAMM Unreviewed; 276 AA.
AC A0A251XCC8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=TPSD3_00780 {ECO:0000313|EMBL:OUD16289.1};
OS Thioflexithrix psekupsensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thioflexithrix.
OX NCBI_TaxID=1570016 {ECO:0000313|EMBL:OUD16289.1, ECO:0000313|Proteomes:UP000194798};
RN [1] {ECO:0000313|EMBL:OUD16289.1, ECO:0000313|Proteomes:UP000194798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OUD16289.1};
RA Fomenkov A., Vincze T., Grabovich M., Anton B.P., Dubinina G., Orlova M.,
RA Belousova E., Roberts R.J.;
RT "Thioflexothrix psekupsii D3 genome sequencing and assembly.";
RL Submitted (DEC-2016) 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:OUD16289.1}.
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DR EMBL; MSLT01000001; OUD16289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251XCC8; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000194798; 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:UP000194798};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT TRANSMEM 59..77
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 57..257
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 142
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 276 AA; 31149 MW; 267542AC45EBFF56 CRC64;
MNWDLATLLV LLVGVSTLIW LYDKLFLERK RLAAQANASK NAAGLDPSET VRVPLMVDLA
RSFLPVFLIV LLLRSFLVEP FRIPSGSMMP TLLIGDFILV NKFSYGFRLP VLNTKVIEMG
KPQRGDVVVF RYPEDTAVPF IKRVVAIPGD HIVYHNANKT IYINGEPMPQ EYIGTYQGVG
SGSNMTGAEQ RLEKLSDVQH EILVLPGRLS PGPYQEMIVP PDEYFVLGDN RDNSRDSRFW
GTVHDEHLIG KAFFIWMNWD SANGGISWPR LGMRIE
//
