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Database: UniProt
Entry: A7GJD2
LinkDB: A7GJD2
Original site: A7GJD2 
ID   PRSA_CLOBL              Reviewed;         336 AA.
AC   A7GJD2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   29-OCT-2014, entry version 50.
DE   RecName: Full=Foldase protein PrsA {ECO:0000255|HAMAP-Rule:MF_01145};
DE            EC=5.2.1.8 {ECO:0000255|HAMAP-Rule:MF_01145};
DE   Flags: Precursor;
GN   Name=prsA {ECO:0000255|HAMAP-Rule:MF_01145};
GN   OrderedLocusNames=CLI_3758;
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F;
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L.,
RA   Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O.,
RA   Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the
CC       post-translocational extracellular folding of several secreted
CC       proteins. {ECO:0000255|HAMAP-Rule:MF_01145}.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000255|HAMAP-Rule:MF_01145}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01145}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01145}.
CC   -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01145}.
CC   -!- SIMILARITY: Contains 1 PpiC domain. {ECO:0000255|HAMAP-
CC       Rule:MF_01145}.
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DR   EMBL; CP000728; ABS42665.1; -; Genomic_DNA.
DR   RefSeq; YP_001392892.1; NC_009699.1.
DR   ProteinModelPortal; A7GJD2; -.
DR   STRING; 441772.CLI_3758; -.
DR   EnsemblBacteria; ABS42665; ABS42665; CLI_3758.
DR   GeneID; 5405141; -.
DR   KEGG; cbf:CLI_3758; -.
DR   PATRIC; 19430413; VBICloBot15611_3597.
DR   eggNOG; COG0760; -.
DR   HOGENOM; HOG000014031; -.
DR   KO; K07533; -.
DR   OMA; KKEFAIN; -.
DR   OrthoDB; EOG6ZH2DM; -.
DR   BioCyc; CBOT441772:GJIE-3715-MONOMER; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01145; Foldase_PrsA; 1.
DR   InterPro; IPR023059; Foldase_PrsA.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Isomerase; Lipoprotein; Membrane;
KW   Palmitate; Rotamase; Signal.
FT   SIGNAL        1     22       {ECO:0000255|HAMAP-Rule:MF_01145}.
FT   CHAIN        23    336       Foldase protein PrsA.
FT                                /FTId=PRO_1000085048.
FT   DOMAIN      194    286       PpiC. {ECO:0000255|HAMAP-Rule:MF_01145}.
FT   LIPID        23     23       N-palmitoyl cysteine. {ECO:0000255|HAMAP-
FT                                Rule:MF_01145}.
FT   LIPID        23     23       S-diacylglycerol cysteine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01145}.
SQ   SEQUENCE   336 AA;  38704 MW;  687E2EDEA4AE8F74 CRC64;
     MKSAKKLLSV LCLGIFILTF TACDMVEKTP EAKAKSTIAK VNGEKIQRKD LDESPNMQQV
     LSQIKTQYGE EFEKTEQGKE VIKEQKKQIL ENLITEKVLL QKGKELKVIP KDEELNKEAD
     KKVNEIKAVY NNDEKKFEET LKSTGFTKET LKEYLKDQIV IEKVINEVTK DVKVEDKDAQ
     KYYNENQSMF TEKPNTMNVS HILVKTEDEA KKVKKRLDAK EDFAKVAKEV SQDTGSKEKG
     GLLGDISYSD SNYDPTFMKA AIALKSGEIS NPVHTQWGYH IIKINSKKEY PVKKFDSVKE
     DIKKQLKQEK QQEAYTKKIE EWKKASKIKT YEKNLL
//
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