ID   NODF_RHILV              Reviewed;          92 AA.
AC   P04685;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Nodulation protein F;
DE   AltName: Full=Host-specificity of nodulation protein A;
GN   Name=nodF; Synonyms=hsnA;
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   STRUCTURE BY NMR.
RX   PubMed=8654592; DOI=10.1016/0014-5793(96)00512-1;
RA   Ghose R., Geiger O., Prestegard J.H.;
RT   "NMR investigations of the structural properties of the nodulation protein,
RT   NodF, from Rhizobium leguminosarum and its homology with Escherichia coli
RT   acyl carrier protein.";
RL   FEBS Lett. 388:66-72(1996).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=11090286; DOI=10.1006/jmbi.2000.4199;
RA   Fowler C.A., Tian F., Al-Hashimi H.M., Prestegard J.H.;
RT   "Rapid determination of protein folds using residual dipolar couplings.";
RL   J. Mol. Biol. 304:447-460(2000).
CC   -!- FUNCTION: Proposed to synthesize nod factor fatty acyl chain. Involved
CC       in trans-2,trans-4,trans-6,cis-11-octadecatetraenoic acid biosynthesis.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-NodF. {ECO:0000305}.
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DR   EMBL; Y00548; CAA68623.1; ALT_SEQ; Genomic_DNA.
DR   PIR; C25095; C25095.
DR   RefSeq; WP_011654221.1; NZ_WIFA01000003.1.
DR   PDB; 1FH1; NMR; -; A=1-92.
DR   PDBsum; 1FH1; -.
DR   AlphaFoldDB; P04685; -.
DR   SMR; P04685; -.
DR   OMA; KIEMNTT; -.
DR   EvolutionaryTrace; P04685; -.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nodulation; Phosphopantetheine; Phosphoprotein; Plasmid.
FT   CHAIN           1..92
FT                   /note="Nodulation protein F"
FT                   /id="PRO_0000180261"
FT   DOMAIN          4..88
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         45
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   HELIX           6..16
FT                   /evidence="ECO:0007829|PDB:1FH1"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:1FH1"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:1FH1"
FT   TURN            77..79
FT                   /evidence="ECO:0007829|PDB:1FH1"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:1FH1"
SQ   SEQUENCE   92 AA;  9945 MW;  F4FF9E92F21F02D4 CRC64;
     MADQLTLEII SAINKLVKAE NGERTSVALG EITTDTELTS LGIDSLGLAD VLWDLEQLYG
     IKIEMNTADA WSNLNNIGDV VEAVRGLLTK EV