ID PRSA_STAEQ Reviewed; 325 AA.
AC Q5HN96;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 01-MAY-2013, entry version 61.
DE RecName: Full=Foldase protein PrsA;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA; OrderedLocusNames=SERP1376;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA Hance I.R., Nelson K.E., Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete
RT genome analysis of an early methicillin-resistant Staphylococcus
RT aureus strain and a biofilm-producing methicillin-resistant
RT Staphylococcus epidermidis strain.";
RL J. Bacteriol. 187:2426-2438(2005).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the
CC post-translocational extracellular folding of several secreted
CC proteins (By similarity).
CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC (omega=0).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (Potential).
CC -!- SIMILARITY: Belongs to the PrsA family.
CC -!- SIMILARITY: Contains 1 PpiC domain.
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DR EMBL; CP000029; AAW54761.1; -; Genomic_DNA.
DR RefSeq; YP_188945.1; NC_002976.3.
DR ProteinModelPortal; Q5HN96; -.
DR STRING; 176279.SERP1376; -.
DR EnsemblBacteria; AAW54761; AAW54761; SERP1376.
DR GeneID; 3242867; -.
DR KEGG; ser:SERP1376; -.
DR PATRIC; 19613619; VBIStaEpi130894_1344.
DR eggNOG; COG0760; -.
DR HOGENOM; HOG000014031; -.
DR KO; K07533; -.
DR OMA; KDNGGQL; -.
DR ProtClustDB; CLSK885597; -.
DR BioCyc; SEPI176279:GJJB-1411-MONOMER; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:HAMAP.
DR GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR HAMAP; MF_01145; Foldase_PrsA; 1; -.
DR InterPro; IPR023059; Foldase_PrsA.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom.
DR SUPFAM; SSF109998; Trigger_fac_C_bac; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; FALSE_NEG.
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 20 Potential.
FT CHAIN 21 325 Foldase protein PrsA.
FT /FTId=PRO_0000042940.
FT DOMAIN 139 245 PpiC.
FT LIPID 21 21 N-palmitoyl cysteine (Potential).
FT LIPID 21 21 S-diacylglycerol cysteine (Potential).
SQ SEQUENCE 325 AA; 36496 MW; 502B3FB3B799EB80 CRC64;
MKLMNKIIVP VTASALLLGA CGSNATESKD NTLISSKAGD VKVADVMKKM GKEQIANTSF
SIVLNKVLAD KYKDKVDTKD IDKDIKKEEK QYGGKDQFES MLKQQGMSLD DYKEQKKLSA
YQKQLLLDKV NVSDKEIKEN SKKTSHILIK VKSKSSDKEG LSDKKAKEKA EKIQKEVEKN
PNKFGEIAKK ESMDSSSAKK DGSLGYVIKG QMVDSFEKAL FKLKEGEVSK VVKTDYGYHI
IKADKETDFN SEKSNIKQKL IEEKVQKKPK LLTDAYKELL KEYKVDYKDR DIKKAIEDSI
LDPDKIKQQQ QQQSQGGSGL TNSGS
//
