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Database: UniProt
Entry: A0A1X7FLJ4_9BACI
LinkDB: A0A1X7FLJ4_9BACI
Original site: A0A1X7FLJ4_9BACI 
ID   A0A1X7FLJ4_9BACI        Unreviewed;       293 AA.
AC   A0A1X7FLJ4; A0A0H4KCN2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=B1B01_17345 {ECO:0000313|EMBL:OXS67257.1}, BEH_04090
GN   {ECO:0000313|EMBL:AKO91360.1}, CJ485_11000
GN   {ECO:0000313|EMBL:RJS65258.1}, SAMN06296056_104262
GN   {ECO:0000313|EMBL:SMF53709.1};
OS   Priestia filamentosa.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=1402861 {ECO:0000313|EMBL:SMF53709.1, ECO:0000313|Proteomes:UP000192915};
RN   [1] {ECO:0000313|EMBL:AKO91360.1, ECO:0000313|Proteomes:UP000036202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hbe603 {ECO:0000313|EMBL:AKO91360.1,
RC   ECO:0000313|Proteomes:UP000036202};
RX   PubMed=26248285;
RA   Jia N., Du J., Ding M.Z., Gao F., Yuan Y.J.;
RT   "Genome Sequence of Bacillus endophyticus and Analysis of Its Companion
RT   Mechanism in the Ketogulonigenium vulgare-Bacillus Strain Consortium.";
RL   PLoS ONE 10:E0135104-E0135104(2015).
RN   [2] {ECO:0000313|Proteomes:UP000036202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hbe603 {ECO:0000313|Proteomes:UP000036202};
RA   Jia N., Du J., Ding M.-Z., Gao F., Yuan Y.-J.;
RT   "Genome Sequence of Bacillus endophyticus and Analysis of its Companion
RT   Mechanism in the Ketogulonigenium vulgare-Bacillus strain Consortium.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AKO91360.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Hbe603 {ECO:0000313|EMBL:AKO91360.1};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000215399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27955 {ECO:0000313|Proteomes:UP000215399};
RA   Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT   "Bacillus sp. V-88(T) DSM27956, whole genome shotgun sequencing project.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|Proteomes:UP000192915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGD-14 {ECO:0000313|Proteomes:UP000192915};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:SMF53709.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27955 {ECO:0000313|EMBL:OXS67257.1}, and SGD-14
RC   {ECO:0000313|EMBL:SMF53709.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:RJS65258.1, ECO:0000313|Proteomes:UP000274910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PK5_39 {ECO:0000313|EMBL:RJS65258.1,
RC   ECO:0000313|Proteomes:UP000274910};
RA   Bokhari A., Bougouffa S., Essack M., Andres-Barrao C., Saad M., Bajic V.B.,
RA   Hirt H.;
RT   "Complete genomes of four Endophytic plant-growth promoting Bacillus that
RT   were isolated from a desert in Pakistan.";
RL   Submitted (AUG-2017) 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       Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC       {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; CP011974; AKO91360.1; -; Genomic_DNA.
DR   EMBL; MWSI01000004; OXS67257.1; -; Genomic_DNA.
DR   EMBL; NQYF01000001; RJS65258.1; -; Genomic_DNA.
DR   EMBL; FXAJ01000004; SMF53709.1; -; Genomic_DNA.
DR   RefSeq; WP_040057125.1; NZ_NQYF01000001.1.
DR   AlphaFoldDB; A0A1X7FLJ4; -.
DR   KEGG; beo:BEH_04090; -.
DR   PATRIC; fig|135735.6.peg.780; -.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000036202; Chromosome.
DR   Proteomes; UP000192915; Unassembled WGS sequence.
DR   Proteomes; UP000215399; Unassembled WGS sequence.
DR   Proteomes; UP000274910; Unassembled WGS sequence.
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; IPR023058; PPIase_PpiC_CS.
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   Pfam; PF13624; SurA_N_3; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01145}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01145};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01145};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036202};
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};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          156..246
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
FT   COILED          69..96
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   293 AA;  33138 MW;  C5F5071D0163AEC6 CRC64;
     MKKLFKRKVM YIILSVALVA LIVCGGWVYS KEQVVASVDG SDITKDDVYN LLADQNGAAA
     VDTLITEKII DKEAEKEDIK ITAKQVNQEL DDLKEQYGGE DTFNQTLEAS GVSLSSLKED
     IKKNKEIEEL LRPSIKITEK EMKEYFNENK DSFAQAAQVK ASHILVDDEK TAKEIKEKLD
     KGEDFATLAK KYSTDTATSE SGGELGYFEE GTMTDEFDKK AFSMKKGEIS DPVKTDYGYH
     IIKVEDVKEA KQASYKDSKA QVKEAIFNEK LQTEYSTWLE KKKKEYDITN SFE
//
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