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Database: UniProt
Entry: F6IHH8_9SPHN
LinkDB: F6IHH8_9SPHN
Original site: F6IHH8_9SPHN 
ID   F6IHH8_9SPHN            Unreviewed;       322 AA.
AC   F6IHH8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN   ORFNames=PP1Y_AT4721 {ECO:0000313|EMBL:CCA91429.1};
OS   Novosphingobium sp. PP1Y.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA91429.1, ECO:0000313|Proteomes:UP000009242};
RN   [1] {ECO:0000313|EMBL:CCA91429.1, ECO:0000313|Proteomes:UP000009242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242};
RX   PubMed=21685292; DOI=10.1128/JB.05349-11;
RA   D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E.,
RA   Paolella G., Di Donato A., Salvatore F.;
RT   "De novo sequencing and assembly of the whole genome of Novosphingobium sp.
RT   strain PP1Y.";
RL   J. Bacteriol. 193:4296-4296(2011).
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; FR856862; CCA91429.1; -; Genomic_DNA.
DR   RefSeq; WP_013831877.1; NC_015580.1.
DR   AlphaFoldDB; F6IHH8; -.
DR   MEROPS; S26.001; -.
DR   KEGG; npp:PP1Y_AT4721; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_1_2_5; -.
DR   OrthoDB; 9815782at2; -.
DR   Proteomes; UP000009242; 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; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
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; PS00760; SPASE_I_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:CCA91429.1};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009242};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          37..274
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   322 AA;  35630 MW;  F010DC3152BC6FF3 CRC64;
     MTEHTADTAS TLCAQESPVS NPDKPKVNWL HELRGLALML LGVLAFHSLI AKPFYIPSIS
     MMPNLLVGDR LVVSKYAYGW NWSSVSFHML PRANWRLFGS TPEYGDIVIV VPGNRKADLI
     KRVVALPGDR IAVVDGRIRL NGKFIPREVE PPVEIAADDA LQCEGDAQPG HCYKGFELYR
     RRLPSGREVY DLPAYRETLP NGATYQVIDY TTQVMDNYPE ITVPEGHVFL MGDDRDRSAD
     SRFPFETDYQ GTPGGGLGGP VPLSDIGGRA EFITFSLDGT QTWNPLSWWS ALREGRALTS
     LRPRIEKHPS DSSTGQPGGN AT
//
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