ID A0A259TYJ1_9BACT Unreviewed; 396 AA.
AC A0A259TYJ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=BSZ36_07560 {ECO:0000313|EMBL:OZC02843.1};
OS Rubricoccus marinus.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubricoccus.
OX NCBI_TaxID=716817 {ECO:0000313|EMBL:OZC02843.1, ECO:0000313|Proteomes:UP000216446};
RN [1] {ECO:0000313|EMBL:OZC02843.1, ECO:0000313|Proteomes:UP000216446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-29 {ECO:0000313|EMBL:OZC02843.1,
RC ECO:0000313|Proteomes:UP000216446};
RA Yoshizawa S., Kumagai Y., Kogure K.;
RT "Study of marine rhodopsin-containing bacteria.";
RL Submitted (NOV-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: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: 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:OZC02843.1}.
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DR EMBL; MQWB01000001; OZC02843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259TYJ1; -.
DR InParanoid; A0A259TYJ1; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000216446; 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; 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; 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; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
DR PROSITE; PS00760; SPASE_I_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000216446}.
FT DOMAIN 41..193
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 338..376
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 70
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 396 AA; 44110 MW; E7DEEDF14A94B79D CRC64;
MPSTPPDASV TPDRPSRKRP GRTTRQRSGR KPEKIKPTFK ENVSFWIKAI VVILFLRAFI
FEPYRIPSES MEDTLLVGDF LIVSKLHYGA RTPNTIGIPF TRIYVPGLVF PQTRLPGFSE
PARGDVAVFN YPAAVDVERG VIPADTPIER RAPYIKRIVA VPGDTLAMVD KMLILNGSPV
PLGATLKQRW RAFSADGDRP TAREMLDMNV QYLEGTDGQA ADGVRQFDIT TTPGGAQLLA
ADPEVARVEP FVLPDSISFS DPRLFDPRAI DLIYDPALAW NADQYGPLVV PGVGMTIDVT
AETMETYADV LEQYEGVEVA EARGGGYLLN GVARDTYTFK ADYYFAMGDN RDNSVDSRYW
GFVPKTHLVG KAVFKFLSFK GEFPFVRPSR FFRPIR
//
