MOSB_RHIML
ID MOSB_RHIML Reviewed; 507 AA.
AC Q07608; Q52890;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Protein MosB;
GN Name=mosB;
OS Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=382;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=L5-30;
RX PubMed=8349559; DOI=10.1128/jb.175.16.5193-5204.1993;
RA Murphy P.J., Trenz S.P., Grzemski W., de Bruijn F.J., Schell J.;
RT "The Rhizobium meliloti rhizopine mos locus is a mosaic structure
RT facilitating its symbiotic regulation.";
RL J. Bacteriol. 175:5193-5204(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RM220-3;
RX PubMed=7551036; DOI=10.1099/13500872-141-7-1683;
RA Rao J.P., Grzemski W., Murphy P.J.;
RT "Rhizobium meliloti lacking mosA synthesizes the rhizopine scyllo-inosamine
RT in place of 3-O-methyl-scyllo-inosamine.";
RL Microbiology 141:1683-1690(1995).
CC -!- FUNCTION: Involved in the biosynthesis of the rhizopine 3-O-methyl-
CC scyllo-inosamine. May have a regulatory role in controlling the
CC housekeeping genes within the nodule which are involved in the
CC biosynthesis of the rhizopine backbone.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR EMBL; L17071; AAA26302.1; -; Genomic_DNA.
DR EMBL; U23753; AAA91313.1; -; Genomic_DNA.
DR PIR; C53308; C53308.
DR AlphaFoldDB; Q07608; -.
DR SMR; Q07608; -.
DR PRIDE; Q07608; -.
DR PATRIC; fig|382.53.peg.1543; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 1.
DR Gene3D; 2.40.50.240; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR009727; NifT.
DR InterPro; IPR024044; NifT/FixU_barrel-like_dom_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244; PTHR30244; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR Pfam; PF06988; NifT; 1.
DR SUPFAM; SSF159203; SSF159203; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR02934; nifT_nitrog; 1.
PE 3: Inferred from homology;
KW DNA-binding; Pyridoxal phosphate; Transcription; Transcription regulation;
KW Two-component regulatory system.
FT CHAIN 1..507
FT /note="Protein MosB"
FT /id="PRO_0000110013"
FT DNA_BIND 256..275
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT MOD_RES 282
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VARIANT 29..32
FT /note="ANED -> EDEA (in strain: RM220-3)"
FT VARIANT 54
FT /note="E -> D (in strain: RM220-3)"
FT VARIANT 67
FT /note="F -> S (in strain: RM220-3)"
FT VARIANT 74
FT /note="A -> P (in strain: RM220-3)"
FT VARIANT 92
FT /note="D -> N (in strain: RM220-3)"
SQ SEQUENCE 507 AA; 55886 MW; 66E88FDBA53FB432 CRC64;
MKVTIRINGD VLSAYIPKKD LEEPIISVAN EDLWGGSILL RNGWRLALPH LPQEARLPVT
VEARRMFGRL DRGAHEKPDR MTRIGEISSS QDAAAMLAEN QKMHPWPALT RTAYEDVAAC
ISSGELSGSG LGIINAFERR MEEWIGGGYV VSASSGTAAL TVALIALGIQ PGDVVLLPSY
TWAATALAPL LIGAIPRFVD IDPNSYNISP TALAAAITPD VKAIIVVHMH GISCDMDEII
CHAREQGIAV IEDCAQAHGA LYKGQHVGLL SDIGCFSMQK SKHLSAGDGG FMVTRDPTLA
QKMRDICNFG LPTPKANYRF DEVVRDGYAV FRECEQIGGM FRLQPMSAAL VMHQLEHLRQ
RIAWLQTAME PLVEESAKIP FFKITRSHVD RTHVWHKIRV GIDYAAVDYF GRSMAEIRRG
LRNSLAERGI SSTLWTAPIL PLQTAFRPYA GVVEWTKSAG HLAIENSFIV FDENYPLIAQ
EPAKMAELVV KLQQAWDEHF TSLARGK
