ARND_SALTY
ID ARND_SALTY Reviewed; 299 AA.
AC O52326;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD {ECO:0000255|HAMAP-Rule:MF_01870};
DE EC=3.5.1.n3 {ECO:0000255|HAMAP-Rule:MF_01870};
GN Name=arnD {ECO:0000255|HAMAP-Rule:MF_01870}; Synonyms=pbgP4, pmrJ;
GN OrderedLocusNames=STM2300;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=9570402; DOI=10.1046/j.1365-2958.1998.00757.x;
RA Gunn J.S., Lim K.B., Krueger J., Kim K., Guo L., Hackett M., Miller S.I.;
RT "PmrA-PmrB-regulated genes necessary for 4-aminoarabinose lipid A
RT modification and polymyxin resistance.";
RL Mol. Microbiol. 27:1171-1182(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10480935; DOI=10.1074/jbc.274.38.27185;
RA Woesten M.M.S.M., Groisman E.A.;
RT "Molecular characterization of the PmrA regulon.";
RL J. Biol. Chem. 274:27185-27190(1999).
RN [4]
RP FUNCTION IN POLYMYXIN RESISTANCE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=11035717; DOI=10.1128/iai.68.11.6139-6146.2000;
RA Gunn J.S., Ryan S.S., Van Velkinburgh J.C., Ernst R.K., Miller S.I.;
RT "Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary
RT for lipopolysaccharide modification, antimicrobial peptide resistance, and
RT oral virulence of Salmonella enterica serovar typhimurium.";
RL Infect. Immun. 68:6139-6146(2000).
CC -!- FUNCTION: Catalyzes the deformylation of 4-deoxy-4-formamido-L-
CC arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-
CC phosphoundecaprenol. The modified arabinose is attached to lipid A and
CC is required for resistance to polymyxin and cationic antimicrobial
CC peptides (Probable). {ECO:0000305|PubMed:11035717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-
CC cis-undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L-
CC arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate;
CC Xref=Rhea:RHEA:27734, ChEBI:CHEBI:15377, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:58909, ChEBI:CHEBI:60463; EC=3.5.1.n3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01870};
CC -!- PATHWAY: Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose
CC undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose
CC undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose
CC and undecaprenyl phosphate: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_01870}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01870}.
CC -!- INDUCTION: Induced by BasR. {ECO:0000269|PubMed:10480935}.
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family. ArnD
CC deformylase subfamily. {ECO:0000255|HAMAP-Rule:MF_01870}.
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DR EMBL; AF036677; AAC04773.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21201.1; -; Genomic_DNA.
DR RefSeq; NP_461242.1; NC_003197.2.
DR RefSeq; WP_000169761.1; NC_003197.2.
DR AlphaFoldDB; O52326; -.
DR STRING; 99287.STM2300; -.
DR PaxDb; O52326; -.
DR EnsemblBacteria; AAL21201; AAL21201; STM2300.
DR GeneID; 1253822; -.
DR KEGG; stm:STM2300; -.
DR PATRIC; fig|99287.12.peg.2435; -.
DR HOGENOM; CLU_084199_0_0_6; -.
DR OMA; KFLWKML; -.
DR PhylomeDB; O52326; -.
DR BioCyc; SENT99287:STM2300-MON; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00496.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule.
DR GO; GO:0036108; P:4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR HAMAP; MF_01870; ArnD; 1.
DR InterPro; IPR023557; ArnD.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Hydrolase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lipopolysaccharide biosynthesis; Reference proteome.
FT CHAIN 1..299
FT /note="Probable 4-deoxy-4-formamido-L-arabinose-
FT phosphoundecaprenol deformylase ArnD"
FT /id="PRO_0000169177"
FT DOMAIN 2..260
FT /note="NodB homology"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01870"
SQ SEQUENCE 299 AA; 33010 MW; 5A33F6D1D494859F CRC64;
MTKVGLRIDV DTLRGTREGV PRLLATLHRH GVQASFFFSV GPDNMGRHLW RLIKPRFLWK
MLRSNAASLY GWDILLAGTA WPGKNIGNAN AGIIRETATY HETGLHAWDH HAWQTHSGHW
SIRQLEEDIA RGITALEAII GKPVTCSAAA GWRADGRVVR AKESFNLRYN SDCRGTTLFR
PLLMPGQTGT PQIPVTLPTW DEVIGPAVQA QSFNTWIISR MLQDKGTPVY TIHAEVEGIV
HQPLFEDLLV RARDAGITFC PLGELLPASP ESLPLGQIVR GHIPGREGWL GCQQAASAS
