ID   PRSA_STRA1              Reviewed;         309 AA.
AC   Q3K1P9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 79.
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}; OrderedLocusNames=SAK_0932;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC   -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC       translocational extracellular folding of several secreted proteins.
CC       {ECO:0000255|HAMAP-Rule:MF_01145}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01145};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01145};
CC       Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_01145}.
CC   -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01145}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000114; ABA45724.1; -; Genomic_DNA.
DR   RefSeq; WP_000857817.1; NC_007432.1.
DR   AlphaFoldDB; Q3K1P9; -.
DR   SMR; Q3K1P9; -.
DR   KEGG; sak:SAK_0932; -.
DR   HOGENOM; CLU_034646_6_0_9; -.
DR   OMA; TMKGSTI; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.50.40; -; 1.
DR   HAMAP; MF_01145; Foldase_PrsA; 1.
DR   InterPro; IPR023059; Foldase_PrsA.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF13145; Rotamase_2; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate; Rotamase;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   CHAIN           23..309
FT                   /note="Foldase protein PrsA"
FT                   /id="PRO_1000085061"
FT   DOMAIN          146..241
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
SQ   SEQUENCE   309 AA;  33877 MW;  9689E74D8D6315A6 CRC64;
     MKTRSKLAAG FLTLMSVATL AACSGKTSNG TNVVTMKGDT ITVSDFYDQV KTSKAAQQSM
     LTLILSRVFD TQYGDKVSDK KVSEAYNKTA KGYGNSFSSA LSQAGLTPEG YKQQIRTTML
     VEYAVKEAAK KELTEANYKE AYKNYTPETS VQVIKLDAED KAKSVLKDVK ADGADFAKIA
     KEKTTATDKK VEYKFDSAGT SLPKEVMSAA FKLDKNGVSD VVSTVDSTTY KTSYYIIKVT
     DKTEKKSDWK SYKNRLKEVI LKDKTSDRAF QNKVISKALE KANVKIKDKA FAGILSQYAT
     TSGSSSLKK