ID A0A0X8G2Z3_9FIRM Unreviewed; 507 AA.
AC A0A0X8G2Z3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=AT726_09475 {ECO:0000313|EMBL:AMC09104.1};
OS Turicibacter sp. H121.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Turicibacteraceae; Turicibacter.
OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC09104.1, ECO:0000313|Proteomes:UP000057144};
RN [1] {ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC09104.1, ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|EMBL:AMC09104.1,
RC ECO:0000313|Proteomes:UP000057144};
RX PubMed=27013036;
RA Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT the Feces of a Contaminated Germ-Free Mouse.";
RL Genome Announc. 4:0-0(2016).
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; Evidence={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; CP013476; AMC09104.1; -; Genomic_DNA.
DR RefSeq; WP_068759471.1; NZ_JAMQUX010000013.1.
DR AlphaFoldDB; A0A0X8G2Z3; -.
DR STRING; 1712675.AT726_09475; -.
DR KEGG; tur:AT726_09475; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000057144; 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; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR47245:SF2; SLR0208 PROTEIN; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000057144};
KW Rotamase {ECO:0000256|HAMAP-Rule:MF_01145, ECO:0000256|PROSITE-
KW ProRule:PRU00278};
KW Signal {ECO:0000256|HAMAP-Rule:MF_01145, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..507
FT /note="Foldase protein PrsA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039362211"
FT DOMAIN 343..437
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 141..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 57524 MW; B2BF0517D01A0000 CRC64;
MKKYFLVTAA LATTLLLGAC SNKDEIGMKL PNGNDNFITS DVANITKQQV FDEMVTDAGL
SALLDLVDYD VLSTKYEIDT AKVDSAIDMY KQMYPEFEDF LLAQGFKNEE ALRQYLELNL
YREAAARAAV TVTDEEIQTA YDEKYKKDEE AESTEESEST NSEETKEIPT LEEVKDELTE
TLIQNKLTDE FIVATLATER EAAGFVLTND FLETQYKEIS TTYEESKETN SSIIAKITDH
EYTVEQLYDE LVPAYGLSDG ISLVDEQILE KKYPVDEKEV KELIDQFKVA YGTNYYQAME
SAGLKTDEEI YNYFKLAQLQ DAALAEAYPI TDEMLQKLYD ETLPKISARH ILVADEETAK
EIIAKLDAAE DKEATFKELA GEYGTDGTKE NGGDLGTFGQ GEMVAEFENA AYALEVGHYS
TEPVKTQFGY HVIYKYAENE KASFEDMKEE LEQTAMKQEY TQLRLETLLI KFRSEANFKF
TDEFLQKRYE TIVANIEESA AQEEAAK
//
