ID   NODE_RHILV              Reviewed;         403 AA.
AC   P04683;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   25-MAY-2022, entry version 96.
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. viciae.
OG   Plasmid sym pRL1JI.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=248;
RX   PubMed=16453679; DOI=10.1002/j.1460-2075.1986.tb04262.x;
RA   Shearman C.A., Rossen L., Johnston A.W.B., Downie J.A.;
RT   "The Rhizobium leguminosarum nodulation gene nodF encodes a polypeptide
RT   similar to acyl-carrier protein and is regulated by nodD plus a factor in
RT   pea root exudate.";
RL   EMBO J. 5:647-652(1986).
RN   [2]
RP   SEQUENCE REVISION TO 27-31.
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).
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; Y00548; CAA68624.1; ALT_SEQ; Genomic_DNA.
DR   PIR; B25095; B25095.
DR   RefSeq; WP_003551798.1; NZ_WIFA01000003.1.
DR   AlphaFoldDB; P04683; -.
DR   SMR; P04683; -.
DR   OMA; MMGHLIA; -.
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; 2.
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..403
FT                   /note="Nodulation protein E"
FT                   /id="PRO_0000180352"
FT   TRANSMEM        329..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        162
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ   SEQUENCE   403 AA;  42110 MW;  782909B074ED75E6 CRC64;
     MDRRVVITGL GGLCGLGTDA SSIWTEMREG RSAIGPISNS EIHELKGMIG TEIKVLPQHD
     IDRKQLISMD RFSLLAVLAA KQAMLQAGLS CNEGNAHRFG ATVGVGFGGW DATEKAYRTL
     LLGGATRTEL FTGVKAMPSA AACQVSMNLG LRGPVFGATS ACASANHAIA SAVDQIKLGR
     ADVMLAGGSD APLVWIVLKA WEAMRVLAPD TCRPFSADRK GLVLGEGAGM AVLESYEHAA
     ARGATMLAEV AGIGLSADAY HIAAPAVHGP EAAMRACLVD ASLNAEDVDY LNAHGTGTKA
     NDQIETTAIK RVFGDHARSM SISSTKSTHA HCLGAASALE MIACVMAIQE GVVPPTANYR
     EPDPDCDLDV TPNVPRERKV RVAMSNAFAM GGMNAVLAFK QVP