ID A0A0B5AQ45_9BACL Unreviewed; 308 AA.
AC A0A0B5AQ45;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=JMA_13360 {ECO:0000313|EMBL:AJD90653.1};
OS Jeotgalibacillus malaysiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=1508404 {ECO:0000313|EMBL:AJD90653.1, ECO:0000313|Proteomes:UP000031449};
RN [1] {ECO:0000313|EMBL:AJD90653.1, ECO:0000313|Proteomes:UP000031449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D5 {ECO:0000313|EMBL:AJD90653.1,
RC ECO:0000313|Proteomes:UP000031449};
RA Yaakop A.S., Chan K.-G., Goh K.M.;
RT "Complete genome of a marine bacteria Jeotgalibacillus malaysiensis.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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; CP009416; AJD90653.1; -; Genomic_DNA.
DR RefSeq; WP_039808296.1; NZ_CP009416.1.
DR AlphaFoldDB; A0A0B5AQ45; -.
DR STRING; 1508404.JMA_13360; -.
DR KEGG; jeo:JMA_13360; -.
DR HOGENOM; CLU_034646_5_3_9; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000031449; 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 Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 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..308
FT /note="Foldase protein PrsA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038553105"
FT DOMAIN 139..229
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 289..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 308 AA; 34541 MW; 61C2BF8F1AF48AE0 CRC64;
MKKWIAAASL TLSVTALAAC SDEEASEVVV STNAGDITKE ELYQEMKTTV GEQALQMMVL
EQILQDKYEV SEEEVDAELE AMKEQYGGQE QFDMILSQQG YTEDTFRDTI RLNRLQEKAL
IEDIEVTEEE VQEKYDQMQK EVNARHILVQ DEETALDVKQ QLEDGADFAE LAREVSTEPA
AQETGGELGF FSAGDMDPAF EDAAFSLEPN VISEPVESSF GWHIIEVTET READIGSFED
MKAEIEHDLK LAKADQTQAS AMIQDMMREA EIDIQDEDLE ATFDAFLSQP EAPAEEEAVE
EETEDTES
//