ID A0A1I2K534_9ACTN Unreviewed; 321 AA.
AC A0A1I2K534;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05216251_12181 {ECO:0000313|EMBL:SFF61543.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF61543.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFF61543.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF61543.1,
RC ECO:0000313|Proteomes:UP000199323};
RA de Groot N.N.;
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}.
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DR EMBL; FONG01000021; SFF61543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2K534; -.
DR STRING; 380248.SAMN05216251_12181; -.
DR Proteomes; UP000199323; 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:UP000199323};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 63..258
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 167
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 321 AA; 33545 MW; 3D87FD21D58D5D3A CRC64;
MTPEGPTGPG GPADVPGPAD RSGGPGGLPE GLPAGPGGPD DPGDGEPSRP SGGSSGKQRS
FWKELPLLVG IALVLALLIK TFLVQAFSIP SDSMQHTLER GDRVLVDKLT PWFGSKPTRG
EVVVFHDPGG WLGENPPAGG NAVTKGIQKG LSFIGLMPSA EEKDLIKRVI GVGGDTVECS
GTGPVKVNGK ALDEPYVFAG NTPCTPDRPF KITVPKNRIW VMGDHRQDSL DSRYHMTLPG
GGTVSDNEVV GRAITVAWPI NRWDWLSIPG TFDQPGINAE GSLAPAAAGF LGAVPLVMLR
RRRLLKAAAP QAGTPAEPED R
//
