PRSA_STRMU
ID PRSA_STRMU Reviewed; 333 AA.
AC Q8CVC6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=SMU_648;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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}.
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DR EMBL; AE014133; AAN58382.1; -; Genomic_DNA.
DR RefSeq; NP_721076.1; NC_004350.2.
DR RefSeq; WP_002261893.1; NC_004350.2.
DR PDB; 7L75; X-ray; 3.15 A; A/B=20-294.
DR PDBsum; 7L75; -.
DR AlphaFoldDB; Q8CVC6; -.
DR SMR; Q8CVC6; -.
DR STRING; 210007.SMU_648; -.
DR PRIDE; Q8CVC6; -.
DR EnsemblBacteria; AAN58382; AAN58382; SMU_648.
DR KEGG; smu:SMU_648; -.
DR PATRIC; fig|210007.7.peg.574; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; TMKGSTI; -.
DR PhylomeDB; Q8CVC6; -.
DR Proteomes; UP000002512; Chromosome.
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 HAMAP; MF_01145; Foldase_PrsA; 1.
DR InterPro; IPR023059; Foldase_PrsA.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Rotamase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT CHAIN 22..333
FT /note="Foldase protein PrsA"
FT /id="PRO_0000029326"
FT DOMAIN 144..237
FT /note="PpiC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT REGION 296..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01145"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 52..70
FT /evidence="ECO:0007829|PDB:7L75"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 106..126
FT /evidence="ECO:0007829|PDB:7L75"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:7L75"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:7L75"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:7L75"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 174..179
FT /evidence="ECO:0007829|PDB:7L75"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:7L75"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:7L75"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7L75"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:7L75"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 249..260
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 264..277
FT /evidence="ECO:0007829|PDB:7L75"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:7L75"
SQ SEQUENCE 333 AA; 36093 MW; 666CA84A5633C54E CRC64;
MKKRTIATGL VTLLSIVTLA ACSKTNQNSK IATMKGDTIT VADFYNEVKN STASKQAVLS
LLVSKVFEKQ YGDKVSDKEV TKAYNEAAKY YGDSFSSALA SRGYTKEDYK KQIRSEKLIE
YAVKEEAKKE ITDASYKSAY KDYKPEVTAQ VIQLDSEDKA KSVLEEAKAD GADFAKIAKD
NTKGDKTEYS FDSGSTNLPS QVLSAALNLD KDGVSDVIKA SDSTTYKPVY YIVKITKKTD
KNADWKAYKK RLKEIIVSQK LNDSNFRNAV IGKAFKKANV KIKDKAFSEI LSQYAAASGS
GSSGSTTTTT AASSAATTAA DDQTTAAETT AAE
