ID A2U0I0_9FLAO Unreviewed; 567 AA.
AC A2U0I0;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:EAQ42041.1};
GN ORFNames=MED152_04965 {ECO:0000313|EMBL:EAQ42041.1};
OS Polaribacter sp. MED152.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ42041.1, ECO:0000313|Proteomes:UP000006470};
RN [1] {ECO:0000313|EMBL:EAQ42041.1, ECO:0000313|Proteomes:UP000006470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ42041.1};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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}.
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DR EMBL; CP004349; EAQ42041.1; -; Genomic_DNA.
DR RefSeq; WP_015480759.1; NC_020830.1.
DR AlphaFoldDB; A2U0I0; -.
DR STRING; 313598.MED152_04965; -.
DR KEGG; pom:MED152_04965; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_0_10; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000006470; 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; 2.
DR InterPro; IPR043739; DUF5684.
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; PF18936; DUF5684; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EAQ42041.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000006470};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT TRANSMEM 540..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 124..285
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 425..507
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 253
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 567 AA; 65384 MW; AD156A0A5464FAE9 CRC64;
MTFTQWFLFF LAVQLIHFLG TWKLYVKAGR KAWEAAVPVY NAVVLMQIIN RPKWWVILLF
IPIVNLLMFP VIWIETIRTF GFYKKLDSLL VIVTLGFYIY YINYAAEANY NAERSLKPRS
ELGEWISSIT FAIIAATLVH TYFMQPFTIP TSSLEKSLLV GDYLFVSKFH YGARVPSTVI
AAPMVHDSLP FTGTKSYLNK PQLPYTRLPG LQKIKNNDIV CFNWPADSLA TMWGDTSGKF
TYKPFDKKTN YVKRSVGIAG DSLEMRDGYI YINGKKNDLP YRAKLQFYYT FESKEPISQS
TFPKFLLDKE RTGVYKILSE YWNNDKVQKA IKENGSLSKI GEDSLYTEVA GGINPQFAQR
LKMINVENKI NINMTAEEVE RLKNYSLTVS IKKVNHGADK AIFPHVEELG WSQDNFGPIY
IPKKGATVAL NSETIPFYEQ IIKNYESNDL AINGEDIFIN GEKATSYTFK QDYYYLIGDN
RHNSLDARYW GYVPFDHVLG KPVMIWFSWD ADAPSFAAKL KSIRWDRMFT TVHGDGEPVS
YRYIVFALIA LYIGYSFYKG KKKKTEK
//
