ID A0A117M1S2_9BACT Unreviewed; 364 AA.
AC A0A117M1S2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
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 ORFNames=XD95_0213 {ECO:0000313|EMBL:KUK79674.1};
OS Microgenomates bacterium 39_7.
OC Bacteria; Candidatus Microgenomates.
OX NCBI_TaxID=1641390 {ECO:0000313|EMBL:KUK79674.1, ECO:0000313|Proteomes:UP000054437};
RN [1] {ECO:0000313|Proteomes:UP000054437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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}.
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:KUK79674.1}.
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DR EMBL; LGGQ01000014; KUK79674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117M1S2; -.
DR PATRIC; fig|1641390.4.peg.749; -.
DR Proteomes; UP000054437; 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 51..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 88..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 162..319
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 226
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 364 AA; 41368 MW; 9486CD4E89C0ACB6 CRC64;
MAISHNQIMK ISKKSIILSF VSWLVCIILF FLITAYTVGV RGELYNETSN FIAYACIGIL
ALGVLSFITG VFFLVLYKLN GNQQKLSLIK TFIGLAIMPL APFYLFLSSI KGLLTKKDSV
SSRLAFLAAS VFTIPIWLFG YFLCYKTIQE FTGLGYDFIE VRDSSSMSPS IPAGSGYKSY
RYKNIWHKLD QSNIYQFQRG DIVSFSNQKS KELIATHGLD NFNFFKRIIA LPGEEVMIAG
GLLFVNGKPL EEPYTLEENN TFTGDIIDED GIVIWQAFFQ ECEKVIVPEN SLFVLGDNRA
HSDDSRIIGF VNFDDVVGYL HINEQKEEYC HGSNCFKHDK EWREVSEFEE SGIERILKQC
DNLI
//
