ID A0A081BLT9_9BACT Unreviewed; 188 AA.
AC A0A081BLT9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=U14_02598 {ECO:0000313|EMBL:GAK51355.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK51355.1};
RN [1] {ECO:0000313|EMBL:GAK51355.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(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}.
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DR EMBL; DF820457; GAK51355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A081BLT9; -.
DR STRING; 1499966.U14_02598; -.
DR HOGENOM; CLU_028723_5_1_0; -.
DR Proteomes; UP000030700; 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; 2.
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; 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};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000030700};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 25..179
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 188 AA; 21195 MW; 9F129F05C0FF4131 CRC64;
MDVTEQEQIS EEESSLTDYK GILYDWGKTI LLSIVIAFAV RVTVVGAYYV PTGSMRPTIG
IGDRLLGWKF VYYFREPHVG EIVVFKPPKE AQADVPRFVK RVVAVAGDVV EVKEGALYVN
GNRQNEPYAS TPYYYMPPMT VPQGHLFVLG DNRNNSADGH VWGFLPEDNV EAKIAFRFWP
LFRAGTVK
//
