ID A0A1Y0GY97_9BACT Unreviewed; 321 AA.
AC A0A1Y0GY97;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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 ORFNames=CCB80_03025 {ECO:0000313|EMBL:ARU40163.1};
OS Armatimonadetes bacterium Uphvl-Ar1.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=2004467 {ECO:0000313|EMBL:ARU40163.1, ECO:0000313|Proteomes:UP000196284};
RN [1] {ECO:0000313|EMBL:ARU40163.1, ECO:0000313|Proteomes:UP000196284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uphvl-Ar1 {ECO:0000313|EMBL:ARU40163.1,
RC ECO:0000313|Proteomes:UP000196284};
RA Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA Dittmann E.;
RT "Draft genome sequences of three Uncultured Armatimonadetes, binned from a
RT Microcystis sp. enrichment culture and from Microcystis bloom
RT metagenomes.";
RL Submitted (MAY-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; CP021423; ARU40163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0GY97; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000196284; Chromosome.
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; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 2.
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:UP000196284};
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 TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 75..307
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 321 AA; 36705 MW; 23DD02309FDFD663 CRC64;
MLTWAGFLLA QSQPNNLILL VDRLARTPIS QIVIFAAVLT AVRLLLYPYL KNTPIHLRSG
IYNFARIIND LADALIYAAI VVFMLVRPFG IQTFYIPSPS MVDTLRTNDY IVANKFVYRT
SDPKFGDIVV FKPSVYARPA DSPDADFIKR CLGVPGDLIE IKDWQVFRNG KPVEEPYKTI
SDQTRGNQLP LAKEEWQPYI DQQEDFKFIQ LDNYKTTDPT EPGNPEGIVP FIFKKDQWSD
QHNFAPRGGS LYNPMMDTNE AVQLPAQRIP KDYYLMIGDN RNGSNDGRYW GLVHRSQIVG
RAEFTWMPIS RAKKLSNPHA K
//
