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Database: UniProt
Entry: A0A0B5AQ45_9BACL
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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
//
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