ID A0A0Q8UNN3_9ACTN Unreviewed; 255 AA.
AC A0A0Q8UNN3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ASE19_20035 {ECO:0000313|EMBL:KRC46604.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC46604.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC46604.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC46604.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC46604.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC46604.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRC46604.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMIP01000015; KRC46604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8UNN3; -.
DR Proteomes; UP000051414; 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; 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 Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000051414}.
FT DOMAIN 3..217
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 33
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 101
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 255 AA; 27547 MW; 4C3A23F95EE83B81 CRC64;
MWQESILLLA VALGLAVLIK AIFVQAFYIP SESMEPGLVK NDRILVQKVS YWFGGTPKRG
DVIVFEDPGE WLGPADAQGP TGFASVLSKV GLYPTGGHLV KRVIGVAGDI VTCCDEQGRI
SVNGKAIDES DYLGPDPGAC NAELLDDWYV EKGTAFSGRC DWTIGPIPAG KVLVLGDNRG
HSADSRAHLC GPDEDPCTQS PWVDTDLVVG KVFTLIWPRD RWRWISRPEV FDDVPDSPPA
DLVEKAKKVG AITGS
//