ID A0A117NVB5_9ACTN Unreviewed; 363 AA.
AC A0A117NVB5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-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=AQI70_34775 {ECO:0000313|EMBL:KUM68053.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM68053.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM68053.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM68053.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
RL Submitted (OCT-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:KUM68053.1}.
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DR EMBL; LMWJ01000033; KUM68053.1; -; Genomic_DNA.
DR RefSeq; WP_062156467.1; NZ_KQ947997.1.
DR AlphaFoldDB; A0A117NVB5; -.
DR STRING; 146536.AQI70_34775; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000054024; 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 Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 56..252
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 85
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 162
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 363 AA; 39670 MW; 65E086CF175E8DF9 CRC64;
MGNRGKPRGV PSSPADNLLP TGSRRAAGPS GGRTRAERRK LQRKVKRRRR RSAIKEIPLL
VGVAVLIALV LKTFLVQAFV IPSGSMEQTI QVGDRVLVDK LTPWFGSKPQ RGDVVVFKDP
GGWLRGEQTT VPKEDPVVVK QVKGALTFIG LLPSDDEKDL IKRVVGVGGD RVKCCDTQGR
VTVNGIPLNE DYLYPGNAPS TTEFDITVPQ GRLWVMGDHR ADSADSRAHQ NQDYGGTVSE
DEVVGRAMVI AWPLGHWSSL EEPKTYASVS DSAAGSTAAP QLSHRVASDD SNGTIQLPSP
AELPLVMGVV GLRRAWGRQR HRVRSWRGGC GGWRTIRARR RGAPRTPRGS SRPGRGRRRD
LRE
//
