ID A0A0P0DPF7_9MICO Unreviewed; 246 AA.
AC A0A0P0DPF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=AOA12_10560 {ECO:0000313|EMBL:ALJ20328.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ20328.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ20328.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ20328.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-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 ---------------------------------------------------------------------------
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; CP012697; ALJ20328.1; -; Genomic_DNA.
DR RefSeq; WP_054682513.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0P0DPF7; -.
DR STRING; 1714373.AOA12_10560; -.
DR KEGG; mio:AOA12_10560; -.
DR PATRIC; fig|1714373.3.peg.2182; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000059097; 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; 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:UP000059097};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 27..50
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 25..222
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 55
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 246 AA; 27079 MW; 2E329ACCF6354DAB CRC64;
MSSDTASGSE AAPRRARRSV WPLLRDIVVI VLVAIVVSFV VKTFVVRSFY IPSGSMQQTL
EIEDRIFVDE LTPRFTGYDR GDVVVFRDPG GWLPVTPRTQ QTPWEGAVDW LLSLVGLSAS
DSKDHLVKRV VGLPGDHVVC CNPIGQVMVN DVPIDETPYL NLDPGQSVPA KKEFDVTVPE
GALWVLGDNR DHSRDSRYNV DQPTHGFVPL DNVVGRAFLI TWPLNRIGFI DGHHDVFAGV
PAPADG
//