ID   NODE_RHILT              Reviewed;         401 AA.
AC   P04684;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Nodulation protein E;
DE   AltName: Full=Host-specificity of nodulation protein B;
DE            EC=2.3.1.-;
GN   Name=nodE; Synonyms=hsnB;
OS   Rhizobium leguminosarum bv. trifolii.
OG   Plasmid sym pRtr843e.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ANU 843;
RX   PubMed=2684629; DOI=10.1002/j.1460-2075.1989.tb08427.x;
RA   Spaink H.P., Weinman J., Djordjevic M.A., Wijffelman C.A., Okker R.J.H.,
RA   Lugtenberg B.J.J.;
RT   "Genetic analysis and cellular localization of the Rhizobium host
RT   specificity-determining NodE protein.";
RL   EMBO J. 8:2811-2818(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RC   STRAIN=ANU 843;
RX   PubMed=3008100; DOI=10.1093/nar/14.7.2891;
RA   Schofield P.R., Watson J.M.;
RT   "DNA sequence of Rhizobium trifolii nodulation genes reveals a reiterated
RT   and potentially regulatory sequence preceding nodABC and nodFE.";
RL   Nucleic Acids Res. 14:2891-2903(1986).
CC   -!- FUNCTION: Proposed to synthesize NOD factor fatty acyl chain. Involved
CC       in the synthesis of a highly unsaturated fatty acid moiety, which forms
CC       part of a lipo-oligosaccharide that is responsible for host
CC       specificity.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
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DR   EMBL; X16620; CAA34617.1; -; Genomic_DNA.
DR   EMBL; X03721; CAA27356.1; -; Genomic_DNA.
DR   PIR; S06021; S06021.
DR   AlphaFoldDB; P04684; -.
DR   SMR; P04684; -.
DR   PRIDE; P04684; -.
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:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd00834; KAS_I_II; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712; PTHR11712; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Nodulation; Plasmid;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..401
FT                   /note="Nodulation protein E"
FT                   /id="PRO_0000180351"
FT   TRANSMEM        329..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   401 AA;  42001 MW;  CA0FB5F8E38188A8 CRC64;
     MDRRVVITGI GGLCGLGTNA ASIWKEMREG PSAISPIITT DLYDLEGTVG LEIKAIPEHD
     IPRKQLVSMD RFSLLAVIAA TEAMKQAGLS CDEQNAHRFG AAMGLGGPGW DTIEETYRSI
     LLDGVTRARI FTAPKGMPSA AAGHVSIFLG LRGPVFGVTS ACAAGNHAIA SAVDQIRLGR
     ADVMLAGGSD APLTWGVLKS WEALRVLAPD TCRPFSADRK GVVLGEGAGM AVLESYEHAA
     ARGATMLAEV AGIGLSGDAY DIVMPSIEGP EAAMRSCLAD AELNPDDVDY LNAHGTGTVA
     NDEMETAAIK RVFGDHAFQM SVSSTKSMHA HCLGAASALE MIACVMAIQE GVIPPTANYR
     EPDPQCDLDV TPNVPREQRC GSMSNAFAMG GTNAVLAFRQ V