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Database: UniProt
Entry: A0YJF8_LYNSP
LinkDB: A0YJF8_LYNSP
Original site: A0YJF8_LYNSP 
ID   A0YJF8_LYNSP            Unreviewed;       367 AA.
AC   A0YJF8;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   ORFNames=L8106_14530 {ECO:0000313|EMBL:EAW38639.1};
OS   Lyngbya sp. (strain PCC 8106) (Lyngbya aestuarii (strain CCY9616)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Lyngbya.
OX   NCBI_TaxID=313612 {ECO:0000313|EMBL:EAW38639.1, ECO:0000313|Proteomes:UP000000737};
RN   [1] {ECO:0000313|EMBL:EAW38639.1, ECO:0000313|Proteomes:UP000000737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC8106 {ECO:0000313|Proteomes:UP000000737};
RA   Stal L., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (DEC-2006) 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|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}.
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:EAW38639.1}.
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DR   EMBL; AAVU01000003; EAW38639.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0YJF8; -.
DR   eggNOG; COG0681; Bacteria.
DR   OMA; DPWLAVN; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000000737; 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; 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   SUPFAM; SSF51306; LexA/Signal peptidase; 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:UP000000737};
KW   Transmembrane {ECO:0000256|RuleBase:RU362042};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT   TRANSMEM        36..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        130..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        186..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          206..358
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        225
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   367 AA;  42204 MW;  F21C4913FAA0DAD1 CRC64;
     MKSQQSITDK EPWLAVSLST VFPGFGQIYA GKTSRGLLLI FITLILFGLN KWLILSPTGS
     VRLGTLLELG DYLLYIFNLF DAYRCTKKAN SREFERLRKD GKDPWKAVFL TRIGPGLGHV
     YVARNGQEQW GFVILFLILV NGADALYSSA EFYQYLQVAI RLLAVCLFSY HAYLSTPTHR
     EKYRRFILGI CLTLLVLDLC SNIVRFSLRE FIFDTHCITQ YDHKSVPPAL EIRDCVVEEK
     ISYHFTNPKR GDIVVFRTTD EMNQNKWNST DVLIKRIIGL PNEKVEVRDG LVYINDKPLN
     ENYIAAEPDD QWGSKVIPDD TYLIFGNNRY RSVGGYSYDH HILVPRDNII GKATKINWPP
     KRMGIIK
//
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