ID A0A437KHI1_9BACI Unreviewed; 297 AA.
AC A0A437KHI1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, entry version 16.
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 ECO:0000313|EMBL:RVT67703.1};
GN ORFNames=EM808_04310 {ECO:0000313|EMBL:RVT67703.1};
OS Niallia taxi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT67703.1, ECO:0000313|Proteomes:UP000288024};
RN [1] {ECO:0000313|EMBL:RVT67703.1, ECO:0000313|Proteomes:UP000288024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT67703.1,
RC ECO:0000313|Proteomes:UP000288024};
RA Tuo L.;
RT "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL Submitted (JAN-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RVT67703.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RZTZ01000001; RVT67703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437KHI1; -.
DR Proteomes; UP000288024; 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 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 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.
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:UP000288024};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..297
FT /note="Foldase protein PrsA"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039692078"
FT DOMAIN 137..227
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 277..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 32982 MW; EDBA636022B60E9B CRC64;
MKKWLLSISL AAGVLALGAC SNDSSDAVVK SDAGNITKDE LYDAMKEKYG ATVLQSLLYE
KVLEDKYKVS DDELNERVDS IKAQLGDNFE LALQQYGYKD EDELRSMIKT GMLQEKAAVK
EVKVTDDEIK AYYDDYKPEI EARHILVADK KTAEEVKKKL DDGEKFEDLA KKYSTDTATK
DKGGDLGWFG AGTMVAEFED AAYKLKVDQI SDPVKTENGY HIIQVTDKKE KGKYEDVKDD
MEYELKVSKL TSDIINSAMA KELEDADVKV EDKDLKSVLD STSADSTSGS TGTSTSK
//
