PRSA_LACLA
ID PRSA_LACLA Reviewed; 308 AA.
AC Q9CEV9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Foldase protein PrsA;
DE EC=5.2.1.8;
DE Flags: Precursor;
GN Name=prsA; Synonyms=pmpA; OrderedLocusNames=LL1725; ORFNames=L164604;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP CHARACTERIZATION.
RC STRAIN=IL1403;
RX PubMed=12147493; DOI=10.1128/aem.68.8.3932-3942.2002;
RA Drouault S., Anba J., Bonneau S., Bolotin A., Ehrlich S.D., Renault P.;
RT "The peptidyl-prolyl isomerase motif is lacking in PmpA, the PrsA-like
RT protein involved in the secretion machinery of Lactococcus lactis.";
RL Appl. Environ. Microbiol. 68:3932-3942(2002).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
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;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: The conserved PPIase motif is absent in this protein but
CC it still has foldase activity.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000305}.
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DR EMBL; AE005176; AAK05823.1; -; Genomic_DNA.
DR PIR; E86840; E86840.
DR RefSeq; NP_267881.1; NC_002662.1.
DR RefSeq; WP_010906107.1; NC_002662.1.
DR PDB; 6VJ2; X-ray; 3.10 A; A/B/C/D=28-308.
DR PDBsum; 6VJ2; -.
DR AlphaFoldDB; Q9CEV9; -.
DR SMR; Q9CEV9; -.
DR STRING; 272623.L164604; -.
DR PaxDb; Q9CEV9; -.
DR EnsemblBacteria; AAK05823; AAK05823; L164604.
DR KEGG; lla:L164604; -.
DR PATRIC; fig|272623.7.peg.1850; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_0_9; -.
DR OMA; TMKGSTI; -.
DR Proteomes; UP000002196; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..308
FT /note="Foldase protein PrsA"
FT /id="PRO_0000029304"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 60..77
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 83..97
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 112..136
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6VJ2"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:6VJ2"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:6VJ2"
FT TURN 296..300
FT /evidence="ECO:0007829|PDB:6VJ2"
SQ SEQUENCE 308 AA; 33832 MW; F9E7FA832E9E0B00 CRC64;
MKFKKLGLVM TTVFAGAALV TLSGCSSSDS ASKDIITMKG DTIRVSDLYK EAKQFPSQPT
NTLLQNLTFD KIFTKDFGKE VTDKDVSKKV KSIKDQYGSQ FSSALQQQGL TEASFTPYMR
TQMLEQAAID HEIKETQYTD ANLKKAWESY HPDVTAYVVS ETSKDAATKA LDAAKKDDAG
KASFEKTNAE SKVTFNSTST SVPTEVQTAA FKLKNGEFSD VIESTSSSTG ATSYYIVEMV
KTSEKGTDMN KYKKELQNVI KTEKEQDTTF VSGVIAKYLK KNNVTVKESA FASLFSQFTQ
TSSSSSSK
