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Database: UniProt
Entry: A0A221W0L1_9PSEU
LinkDB: A0A221W0L1_9PSEU
Original site: A0A221W0L1_9PSEU 
ID   A0A221W0L1_9PSEU        Unreviewed;       319 AA.
AC   A0A221W0L1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-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   Name=lepB {ECO:0000313|EMBL:ASO19307.1};
GN   ORFNames=AHOG_08310 {ECO:0000313|EMBL:ASO19307.1}, FHR81_001575
GN   {ECO:0000313|EMBL:MBB5920545.1};
OS   Actinoalloteichus hoggarensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinoalloteichus.
OX   NCBI_TaxID=1470176 {ECO:0000313|EMBL:ASO19307.1, ECO:0000313|Proteomes:UP000204221};
RN   [1] {ECO:0000313|EMBL:ASO19307.1, ECO:0000313|Proteomes:UP000204221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45943 {ECO:0000313|EMBL:ASO19307.1,
RC   ECO:0000313|Proteomes:UP000204221};
RA   Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA   Kalinowski J., Zotchev S.B.;
RT   "Complete genome sequence of Actinoalloteichus hoggarensis DSM 45943, type
RT   strain of Actinoalloteichus hoggarensis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB5920545.1, ECO:0000313|Proteomes:UP000541573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8639 {ECO:0000313|EMBL:MBB5920545.1,
RC   ECO:0000313|Proteomes:UP000541573};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (AUG-2020) 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}.
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DR   EMBL; CP022521; ASO19307.1; -; Genomic_DNA.
DR   EMBL; JACHJM010000002; MBB5920545.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221W0L1; -.
DR   KEGG; ahg:AHOG_08310; -.
DR   Proteomes; UP000204221; Chromosome.
DR   Proteomes; UP000541573; 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, ECO:0000313|EMBL:ASO19307.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000204221};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        66..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          63..265
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   319 AA;  34715 MW;  E6AF471F8880C42B CRC64;
     MADLVPSTSP QGESDQPNPS DRPSEWQHRD HAGGAGHSGP SSADDADDGR EKPSKPAKKG
     SFWRELFVLV GIAVVLTIVI QTFLARVYVI PSQSMEETLH GCAGCTNDRV LVDKITYRFT
     DPEPGDVVVF RGPEAWGQND FMTAEPANPV ARFVQNVGAM FGFAQPDEKD FVKRVIATGG
     QTVECCDEEN RVLVDGDPLD EPYIFWQPGR GNTQEPFGPV TVPDDHIWMM GDNRNNSLDS
     RVQGGGGELG AVPLDNVIGK ARIVVLPPQR WQGISDHDPQ QSVLSAPAWQ AAVPAGLGLL
     GAFPTLWLGR RLLGRRDRD
//
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