ID U5S7U8_9LACT Unreviewed; 337 AA.
AC U5S7U8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Foldase protein PrsA {ECO:0000256|HAMAP-Rule:MF_01145};
DE EC=5.2.1.8 {ECO:0000256|HAMAP-Rule:MF_01145};
GN Name=prsA {ECO:0000256|HAMAP-Rule:MF_01145};
GN ORFNames=Q783_03160 {ECO:0000313|EMBL:AGY81300.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81300.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY81300.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY81300.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
CC -!- FUNCTION: Plays a major role in protein secretion by helping the post-
CC translocational extracellular folding of several secreted proteins.
CC {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|HAMAP-
CC Rule:MF_01145};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193,
CC ECO:0000256|HAMAP-Rule:MF_01145}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004193, ECO:0000256|HAMAP-Rule:MF_01145}.
CC Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the PrsA family. {ECO:0000256|ARBA:ARBA00006071,
CC ECO:0000256|HAMAP-Rule:MF_01145}.
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DR EMBL; CP006812; AGY81300.1; -; Genomic_DNA.
DR RefSeq; WP_023177256.1; NC_022606.1.
DR AlphaFoldDB; U5S7U8; -.
DR STRING; 1266845.Q783_03160; -.
DR KEGG; caw:Q783_03160; -.
DR PATRIC; fig|1266845.5.peg.574; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_1_9; -.
DR Proteomes; UP000017469; 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 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 PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01145};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01145};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_01145};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01145};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_01145};
KW Rotamase {ECO:0000256|HAMAP-Rule:MF_01145, ECO:0000256|PROSITE-
KW ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_01145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..337
FT /note="Foldase protein PrsA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038587475"
FT DOMAIN 137..227
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 286..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..337
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 36428 MW; C609563C2449CD9A CRC64;
MKKLLLATAT ILAGLTIAGC SDSTVASSTA GKITEDEFYE AMKETVGTSM LQQLIIEDVL
TDLYGDKVTD EVVDKQYSTE EENYGGAEAF EYIMLQQGYT ADSYKDTIRL NLLIEAAVKD
KTDFTDEEIQ AAYDEYVPEV TAAHILVEDE ETAKDIINQL NDGADFAELA KEYSTDTATA
ENGGEVTFSS GEMVPEFEEA AYALKDGETT TEPVATDYGF HVIKMIEKPE KGTLEEETDT
IKDQLITTKL ADSASIQAVI SGIMKDANII IDDKDLSTAM DAYLGTEEST TEESAVEESA
VDESATDESA VDESAVDESA VDESAVDESA VEESATE
//
