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Database: UniProt
Entry: A0A1H2EQ95_9FLAO
LinkDB: A0A1H2EQ95_9FLAO
Original site: A0A1H2EQ95_9FLAO 
ID   A0A1H2EQ95_9FLAO        Unreviewed;       567 AA.
AC   A0A1H2EQ95;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   ORFNames=SAMN04487762_1011 {ECO:0000313|EMBL:SDT97261.1};
OS   Polaribacter sp. Hel1_33_78.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1336804 {ECO:0000313|EMBL:SDT97261.1, ECO:0000313|Proteomes:UP000198843};
RN   [1] {ECO:0000313|EMBL:SDT97261.1, ECO:0000313|Proteomes:UP000198843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_33_78 {ECO:0000313|EMBL:SDT97261.1,
RC   ECO:0000313|Proteomes:UP000198843};
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|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; LT629794; SDT97261.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2EQ95; -.
DR   STRING; 1336804.SAMN04487762_1011; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000198843; Chromosome i.
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};
KW   Membrane {ECO:0000256|RuleBase:RU362042};
KW   Protease {ECO:0000256|RuleBase:RU362042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198843};
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        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        86..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        125..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        541..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          124..284
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          468..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;  65476 MW;  48D2C1AFDCF2016D CRC64;
     MTFTQWFIFF LVVQVIHFLG TWKLYVKAGR KAWEAAVPVY NGIVLMQIIN RPKWWVILLF
     VPVVNLLMFP VIWIETIRTF GFYKKLESFL VIATLGLYIF YINYNTDAEY NAERSIKPRS
     ELGEWVSSIA FAIIAATLVH TYFMQPFTIP TSSLEKSLLV GDYLFVSKFH YGARVPSTVI
     AAPMVHDSLP FTGTASYLKK PQLPYTRLPG LQKIKNNDIV CFNWPADSLA TMWGDTSGKF
     TYKPVDKKTN YVKRSVGIAG DSLEMRNGYF FINGKKNELP YRAKLQFYYT FECKQPISQS
     TYPKFLLNKE KTGVYKILSE YWNNDKVQEA IKKNGNLSKI GEDSLYTEVA GGVNPQFAQR
     LKMINVDHKI NINLTEEEVI RLEKYPLTVS VKKINHSPDN AIFPHVKKLG WSQDNFGPIY
     IPKKGATVKL DSESIPFYKQ IIKNYESNDL VINGEDIFIN GEKTDSYTFK QDYFYLIGDN
     RHNSLDARYW GYVPFDHVLG KPVMIWFSWD ANAPSFTAKL KSIRWNRMFT TVGGDGEPIS
     YRYFVFALIA LYIGYSFYKG KKKTSKK
//
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