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Database: UniProt
Entry: I7LA11_9LACO
LinkDB: I7LA11_9LACO
Original site: I7LA11_9LACO 
ID   I7LA11_9LACO            Unreviewed;       304 AA.
AC   I7LA11;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=BN55_00660 {ECO:0000313|EMBL:CCI81849.1};
OS   Lactobacillus hominis DSM 23910 = CRBIP 24.179.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1423758 {ECO:0000313|EMBL:CCI81849.1, ECO:0000313|Proteomes:UP000009320};
RN   [1] {ECO:0000313|EMBL:CCI81849.1, ECO:0000313|Proteomes:UP000009320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRBIP 24.179T {ECO:0000313|Proteomes:UP000009320};
RA   Cousin S., Ma L., Bizet C., Loux V., Bouchier C., Clermont D., Creno S.;
RT   "Draft Genome Sequence of Lactobacillus hominis Strain CRBIP 24.179T,
RT   isolated from human intestine.";
RL   Submitted (JUN-2012) 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:CCI81849.1}.
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DR   EMBL; CAKE01000010; CCI81849.1; -; Genomic_DNA.
DR   RefSeq; WP_008470759.1; NZ_CAKE01000010.1.
DR   AlphaFoldDB; I7LA11; -.
DR   STRING; 1423758.FC41_GL000943; -.
DR   GeneID; 82847087; -.
DR   PATRIC; fig|1423758.3.peg.954; -.
DR   eggNOG; COG0760; Bacteria.
DR   OrthoDB; 14196at2; -.
DR   Proteomes; UP000009320; 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; IPR027304; Trigger_fact/SurA_dom_sf.
DR   PANTHER; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00639; Rotamase; 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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..304
FT                   /note="Foldase protein PrsA"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038922452"
FT   DOMAIN          143..236
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   304 AA;  34106 MW;  1E570D9B461794F6 CRC64;
     MKKKYKLSVL ALISISLLGV GVSGCSNNSE VAQYGNNKKI TQQDFYNELK QNPASKTVLA
     NMLIYDALKE AYGNKVNQAE INKTYDAYKN QYGVQFNAFL ENNNYTRKSF KQLIEINYLS
     KAALKAQMKP TQAQLKAEWK NYQPKITVQH ILTTKAETAN EVVSKLDAGA SFDSLANEYS
     VDNTTSTKGG KLAPFNMTDK KYDTAFKKAA YKLKDGEYTS QPVQVTTGYE IIKMIKHPAK
     GSFSANKKAL TQELYDKWAN NSTIMQNVIS QVLKDQKVEI KDKDLKSALD QYKGKTNSAN
     KITK
//
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