ID   LPPX_PAEBA              Reviewed;         280 AA.
AC   V9TSX0;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Chaperone protein LppX {ECO:0000303|PubMed:24549767};
DE   Flags: Precursor;
GN   Name=lppX {ECO:0000303|PubMed:24549767, ECO:0000312|EMBL:AHC74024.1};
GN   ORFNames=DFQ00_11066 {ECO:0000312|EMBL:PYE48004.1};
OS   Paenibacillus barcinonensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=198119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=24549767; DOI=10.1007/s00253-014-5565-2;
RA   Valenzuela S.V., Diaz P., Pastor F.I.;
RT   "Xyn11E from Paenibacillus barcinonensis BP-23: a LppX-chaperone-dependent
RT   xylanase with potential for upgrading paper pulps.";
RL   Appl. Microbiol. Biotechnol. 98:5949-5957(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15478 / BCRC 17560 / CECT 7022 / CIP 108718 / BP-23;
RX   PubMed=26203337; DOI=10.1186/s40793-015-0017-x;
RA   Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA   De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA   Kyrpides N.C.;
RT   "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT   the genomes of soil and plant-associated and newly described type
RT   strains.";
RL   Stand. Genomic Sci. 10:26-26(2015).
CC   -!- FUNCTION: Is required for the expression of the adjacently encoded
CC       xylanase Xyn11E in an active form. LppX seems to act as a specific
CC       chaperone necessary for the correct folding of the xylanase during
CC       secretion across the cytoplasmic membrane.
CC       {ECO:0000269|PubMed:24549767}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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; KF766535; AHC74024.1; -; Genomic_DNA.
DR   EMBL; QJSW01000010; PYE48004.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9TSX0; -.
DR   SMR; V9TSX0; -.
DR   EnsemblBacteria; PYE48004; PYE48004; DFQ00_11066.
DR   Proteomes; UP000247790; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR   Gene3D; 3.90.1580.10; -; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Chaperone; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..280
FT                   /note="Chaperone protein LppX"
FT                   /id="PRO_5016557793"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   280 AA;  31488 MW;  11725ED3CAE6AE08 CRC64;
     MRKWLIFLLI AAVAGLSACS TSGNTTVSDD LVLVEGGAFK TSKSSYSDKN VTLSDFYIGK
     YEVTQKQWMD VMGDNPSGFK GEERPVERVT WYDAIEYCNA RSIKENLKPY YTIDKETTDP
     DNKNENDNIK WTVTINEGAN GYRLPTGAEW EYAASGGQKS QNFTYSGSNN PDEVAWYWMN
     AGEKPLTGDW NWPAIENNRN QTKPVGQQKA NELGIYDMSG NVREWCWEWH SHPETPENTW
     RISKGGGWVS SVNTAEISYP GKFDANGLGP DQGLRVVRSK