LPXF_BACTN
ID LPXF_BACTN Reviewed; 225 AA.
AC Q8A6M3;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Lipid A 4'-phosphatase {ECO:0000303|PubMed:25574022};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxF {ECO:0000303|PubMed:25574022}; OrderedLocusNames=BT_1854;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
RN [3]
RP LIPID A STRUCTURE.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=20974832; DOI=10.1128/iai.00937-10;
RA Coats S.R., Berezow A.B., To T.T., Jain S., Bainbridge B.W., Banani K.P.,
RA Darveau R.P.;
RT "The lipid A phosphate position determines differential host Toll-like
RT receptor 4 responses to phylogenetically related symbiotic and pathogenic
RT bacteria.";
RL Infect. Immun. 79:203-210(2011).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=25574022; DOI=10.1126/science.1260580;
RA Cullen T.W., Schofield W.B., Barry N.A., Putnam E.E., Rundell E.A.,
RA Trent M.S., Degnan P.H., Booth C.J., Yu H., Goodman A.L.;
RT "Gut microbiota. Antimicrobial peptide resistance mediates resilience of
RT prominent gut commensals during inflammation.";
RL Science 347:170-175(2015).
CC -!- FUNCTION: Probably removes the 4'-phosphate group from lipid A. Removal
CC of this phosphate group confers resistance to cationic antimicrobial
CC peptides (CAMPs), inflammation-associated peptides produced by the
CC human host. This LPS modification helps maintain the stability of this
CC commensal bacterium in gut microbiota. {ECO:0000305|PubMed:25574022}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:A0Q4N6}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in the absence of host gut
CC inflammation. Loss of resistance to the cationic antimicrobial peptide
CC polymyxin B (PMB). Lipid A is bi- rather than mono-phosphorylated, with
CC mass corresponding to a 1- 4'-phosphorylated molecule. Increased
CC negative charge on the cell surface leading to greater binding of PMB,
CC increased outer membrane disruption by PMB. Decreased survival
CC (fitness) in host (mouse) cells after infection with C.rodentium (a
CC mouse enteropathogen that induces inflammation) or in mice subjected to
CC other inflammation-producing stimuli. {ECO:0000269|PubMed:25574022}.
CC -!- MISCELLANEOUS: In this organism the major lipid A structure is a
CC pentaacylated disaccharide of glucosamine with a single phosphate at
CC the 1- position. {ECO:0000269|PubMed:20974832}.
CC -!- SIMILARITY: Belongs to the lipid A LpxF 4'-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AE015928; AAO76961.1; -; Genomic_DNA.
DR RefSeq; NP_810767.1; NC_004663.1.
DR RefSeq; WP_011108022.1; NC_004663.1.
DR AlphaFoldDB; Q8A6M3; -.
DR SMR; Q8A6M3; -.
DR STRING; 226186.BT_1854; -.
DR PaxDb; Q8A6M3; -.
DR PRIDE; Q8A6M3; -.
DR EnsemblBacteria; AAO76961; AAO76961; BT_1854.
DR GeneID; 60927842; -.
DR KEGG; bth:BT_1854; -.
DR PATRIC; fig|226186.12.peg.1904; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_072573_10_0_10; -.
DR InParanoid; Q8A6M3; -.
DR OMA; FYSAHAS; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane; Hydrolase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..225
FT /note="Lipid A 4'-phosphatase"
FT /id="PRO_0000432494"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
SQ SEQUENCE 225 AA; 25230 MW; 8D8F420E14C210D9 CRC64;
MIEFLSDIDT QLLLFFNGIH SPFWDYFMSA FTGKVIWVPM YASILYILLK NFHWKVALCY
VVAIALTITF ADQMCNSFLR PLVGRLRPSN PENPIADLVY IVNGRRGGGF GFPSCHAANS
FGLAIFLICL FRKRWLSIFI VLWAFTNSYT RLYLGLHYPG DLVAGAIIGG FGGWLFYFIA
HKLTARLQSD TPVPGKGAGM KQTEVMIYTG LLTLAGIIIY SIVQS
