LPXF_RHIEC
ID LPXF_RHIEC Reviewed; 257 AA.
AC Q2KA78;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Lipid A 4'-phosphatase {ECO:0000303|PubMed:20153447};
DE EC=3.1.-.- {ECO:0000305};
GN Name=lpxf {ECO:0000303|PubMed:20153447}; OrderedLocusNames=RHE_CH01455;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND ANTIBIOTIC RESISTANCE.
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=20153447; DOI=10.1016/j.bbalip.2010.02.001;
RA Ingram B.O., Sohlenkamp C., Geiger O., Raetz C.R.;
RT "Altered lipid A structures and polymyxin hypersensitivity of Rhizobium
RT etli mutants lacking the LpxE and LpxF phosphatases.";
RL Biochim. Biophys. Acta 1801:593-604(2010).
CC -!- FUNCTION: Probably removes the 4'-phosphate moiety from lipid A
CC species. Not seen to act on other membrane components, nor does it
CC dephosphorylate the 1-phosphate group of lipid A and/or lipid A
CC precursors. {ECO:0000305|PubMed:20153447}.
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: Lipid A contains a monophosphate group at
CC position 4' instead of the usual galacturonic acid moiety. No longer
CC has 4'-dephosphorylase activity on Kdo(2)-lipid IV(A). Increased
CC sensitivity to the cationic antimicrobial peptide (CAMP) polymyxin B
CC (PMB) but not to other several other antibiotics. A double lpxE-lpxF
CC mutant contains lipid A bi-phosphorylated at positions 1- and 4'- and
CC has greater sensitivity to PMB than either single mutant. No visible
CC effect on free-living bacteria, or on nitrogen fixation upon nodulation
CC of P.vulgaris. {ECO:0000269|PubMed:20153447}.
CC -!- MISCELLANEOUS: In this strain lipid A lacks phosphate groups, instead
CC contains a galacturonic acid moiety at position-4' in place of the
CC monophosphate group found in E.coli. {ECO:0000305|PubMed:20153447}.
CC -!- SIMILARITY: Belongs to the lipid A LpxF 4'-phosphatase family.
CC {ECO:0000305}.
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DR EMBL; CP000133; ABC90258.1; -; Genomic_DNA.
DR RefSeq; WP_011424788.1; NC_007761.1.
DR AlphaFoldDB; Q2KA78; -.
DR SMR; Q2KA78; -.
DR STRING; 347834.RHE_CH01455; -.
DR EnsemblBacteria; ABC90258; ABC90258; RHE_CH01455.
DR GeneID; 61479915; -.
DR KEGG; ret:RHE_CH01455; -.
DR eggNOG; COG0671; Bacteria.
DR HOGENOM; CLU_070327_1_0_5; -.
DR OMA; FGAHYLS; -.
DR UniPathway; UPA00973; -.
DR Proteomes; UP000001936; 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..257
FT /note="Lipid A 4'-phosphatase"
FT /id="PRO_0000432497"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 28363 MW; 1E465E0933FC671D CRC64;
MTAFSKHRWR GPVIRRPKTT FGAFLLLFWT WWALLAVFRA FPGIDIYFSQ LFFLGTDCDA
TAAAGSICGG FPYRDSGNFD LLRTIFFRLP YVVAIVMAWK LIECYQQHGA TFNAERARKL
KVGLGALLIG PVLLVNVILK EHWGRPRPVQ TDIFGGALHF VEAGSLAGKC VSNCSFVSGE
AASAGWLFCL LLFVPKSLRY ALVPPVAAIS ILTPAMRLSF GAHYLSDVTL GWLSSLVVFA
ALLALTESQQ HQKNSEI
