ID A0A060RAT6_9BACT Unreviewed; 299 AA.
AC A0A060RAT6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=BN938_2681 {ECO:0000313|EMBL:CDN32750.1};
OS Mucinivorans hirudinis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Mucinivorans.
OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN32750.1, ECO:0000313|Proteomes:UP000027616};
RN [1] {ECO:0000313|EMBL:CDN32750.1, ECO:0000313|Proteomes:UP000027616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|Proteomes:UP000027616};
RX PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA Nelson M.C., Bomar L., Graf J.;
RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT hirudinis M3T.";
RL Genome Announc. 3:e01530-e01514(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; HG934468; CDN32750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060RAT6; -.
DR STRING; 1433126.BN938_2681; -.
DR KEGG; rbc:BN938_2681; -.
DR PATRIC; fig|1433126.3.peg.2654; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR Proteomes; UP000027616; Chromosome I.
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; 2.
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; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
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, ECO:0000313|EMBL:CDN32750.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000027616};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 14..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 23..139
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 243..279
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 49
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 299 AA; 34429 MW; BEB8F5AFC0B18CDC CRC64;
MLDPDKYEKI FKKFYFFFLA IFVIFILFLA VKFGTRIFVY DSFGIPTDSM QPTLMPGDMV
YADKLTFGAR LYDNLDSAAK SRNPATTRVG GFGKIKHNDV LIFNFPVPYS WSKIEFNIRR
VYCKRCVALP GDTISIVNGF FKNSSTADTL GYIPAQKRLS LIPEDMLADG IRRAYPFDSV
NYNWTIKNFG PLYIPARGSR VALDTVNYLL YRLAVEYETG LRLTVRDSVL YLGNEPVSEY
VFTENYYFTA GDNAENSQDS RYWGLLPEKH IIGIAKSILY SKSKVNDKFR RDRLLKKIE
//
