ID   NOLL_RHILO              Reviewed;         373 AA.
AC   Q52778;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Nodulation protein NolL;
DE            EC=2.3.1.-;
GN   Name=nolL; OrderedLocusNames=mlr8757;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NZP 2213;
RX   PubMed=8850088; DOI=10.1094/mpmi-9-0187;
RA   Scott D.B., Young C.A., Collins-Emerson J.M., Terzaghi E.A., Rockman E.S.,
RA   Lewis P.E., Pankhurst C.E.;
RT   "Novel and complex chromosomal arrangement of Rhizobium loti nodulation
RT   genes.";
RL   Mol. Plant Microbe Interact. 9:187-197(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Thought to be an acetyltransferase that modifies the fucose
CC       of the nod factor.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. {ECO:0000305}.
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DR   EMBL; U22899; AAB50273.1; -; Genomic_DNA.
DR   EMBL; BA000012; BAB52514.1; -; Genomic_DNA.
DR   RefSeq; WP_010913835.1; NC_002678.2.
DR   AlphaFoldDB; Q52778; -.
DR   KEGG; mlo:mlr8757; -.
DR   eggNOG; COG3594; Bacteria.
DR   HOGENOM; CLU_741613_0_0_5; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   PANTHER; PTHR37312; MEMBRANE-BOUND ACYLTRANSFERASE YKRP-RELATED; 1.
DR   PANTHER; PTHR37312:SF1; MEMBRANE-BOUND ACYLTRANSFERASE YKRP-RELATED; 1.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Cell membrane; Membrane; Nodulation; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..373
FT                   /note="Nodulation protein NolL"
FT                   /id="PRO_0000208082"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        4
FT                   /note="N -> H (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="G -> A (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="M -> T (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="S -> L (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="I -> M (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="W -> S (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        221
FT                   /note="L -> F (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="Q -> R (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268
FT                   /note="A -> R (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="T -> A (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        362
FT                   /note="R -> H (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        365
FT                   /note="L -> P (in Ref. 1; AAB50273)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   373 AA;  41866 MW;  24D21ED82AA232AF CRC64;
     MLDNIRAGAK GRGSCPAGTN NRDLSFDFAK GILITLVIIG HLLQYLIYQG TDAFWLSPYF
     KSIYMFHMPL FMAISGYLSS GAILRKSFTQ GVGERAMQLL LPMLFWCTLI WTLKSAVIFP
     MKSLTDTLLD LSTEVIGTYW FIWAAFISFI LIRVLTTFNR LSIWIISASA IAVAFAPITL
     SITPLLKYTY PFYCLGFLFA QPIGWQNGVI WRYKWIFVVL LSIAAFICFL GWGKETYAYN
     NLVLIHDEQS AKQVFLMFSG SLAASAVAMQ SMFQCWRLVY STRVARFVAV QLGQSTLLLY
     LVQGAVFRLM DLIQFGEVWN LTTRITFATV LGVAIVVIAM AIRSIARNLG YVSRIVVGAP
     PRPSLLKSQS VIN
//