ID A0A1G4YIP2_9ACTN Unreviewed; 305 AA.
AC A0A1G4YIP2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN03159343_2930 {ECO:0000313|EMBL:SCX53175.1};
OS Klenkia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=1960309 {ECO:0000313|EMBL:SCX53175.1, ECO:0000313|Proteomes:UP000198981};
RN [1] {ECO:0000313|Proteomes:UP000198981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45722 {ECO:0000313|Proteomes:UP000198981};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR EMBL; FMUH01000004; SCX53175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4YIP2; -.
DR STRING; 1960309.SAMN03159343_2930; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000198981; 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 Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 54..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 279..297
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 50..249
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 305 AA; 33189 MW; CE20FC95E51D4C25 CRC64;
MSTDRPTGPA DDETAGHRAE GGADEVRVGR FSRRARRRDR EEQKKSSLLR ELPVLLVVAF
VLALLVKTFL VQAFFIPSGS MEQTLHGCTG CTGDRVLVTK PPYWFSDPEP GDIVVFQGPD
TWTPEVQVAE PDNWFSSAAL FLGRAIGVAP PSEDDYVKRV IATGGQTVQC CDEQGRILVD
GEPLDEPYIY ENNPLESRSF GPVVVPEGRL WVMGDHRSAS ADSRSHVGDQ YAGTIGVDDV
IGKASVIVWP FSRFAFLDSP DIQQQQAAGA SVTPVQADVV AAAPLLLGLA GAVPVAARRR
RRRHR
//
