NODE_RHIME
ID NODE_RHIME Reviewed; 402 AA.
AC P06230;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 123.
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; OrderedLocusNames=RA0466; ORFNames=SMa0853;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=3020515; DOI=10.1093/nar/14.18.7453;
RA Debelle F., Sharma S.B.;
RT "Nucleotide sequence of Rhizobium meliloti RCR2011 genes involved in host
RT specificity of nodulation.";
RL Nucleic Acids Res. 14:7453-7472(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=17246400; DOI=10.1093/genetics/117.2.191;
RA Fisher R.F., Swanson J.A., Mulligan J.T., Long S.R.;
RT "Extended region of nodulation genes in Rhizobium meliloti 1021. II.
RT Nucleotide sequence, transcription start sites and protein products.";
RL Genetics 117:191-201(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; X04379; CAA27961.1; -; Genomic_DNA.
DR EMBL; Y00604; CAA68648.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65124.1; -; Genomic_DNA.
DR PIR; B24706; B24706.
DR PIR; B95320; B95320.
DR RefSeq; NP_435712.1; NC_003037.1.
DR RefSeq; WP_010967448.1; NC_003037.1.
DR AlphaFoldDB; P06230; -.
DR SMR; P06230; -.
DR EnsemblBacteria; AAK65124; AAK65124; SMa0853.
DR GeneID; 61599269; -.
DR KEGG; sme:SMa0853; -.
DR PATRIC; fig|266834.11.peg.475; -.
DR HOGENOM; CLU_000022_69_2_5; -.
DR OMA; STHAHCI; -.
DR Proteomes; UP000001976; Plasmid pSymA.
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 InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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 Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..402
FT /note="Nodulation protein E"
FT /id="PRO_0000180353"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
SQ SEQUENCE 402 AA; 41827 MW; A2193F6D94C91D2D CRC64;
MDRRVVITGM GGLCGLGTDT TSIWKWMREG RSAIGPLLNT ELHGLKGIVG AEVKALPDHN
IDRKQLVSMD RISVLAVIAA HEAMRQAGLS CNEGNALRFG ATVGVGLGGW DATEKAYRTL
LVDGGTRTEI FTGVKAMPSA AACQVSMSLG LRGPVFGVTS ACSSANHAIA SAVDQIKCGR
ADVMLAGGSD APLVWIVLKA WEAMRALAPD TCRPFSAGRK GVVLGEGAGM AVLESYEHAT
ARGATILAEV AGVGLSADAF HITAPAVHGP ESAMRACLAD AGLNAEDVDY LNAHGTGTKA
NDQNETTAIK RVFGDHAYSM SISSTKSTHA HCIGAASALE MIACVMAIQE GVVPPTANYR
EPDPDCDLDV TPNVPRERKV RVAMSNAFAM GGTNAVLAFK QV
