MGLA_MYXXD
ID MGLA_MYXXD Reviewed; 195 AA.
AC Q1DB04; Q50884;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Mutual gliding-motility protein MglA;
GN Name=mglA; OrderedLocusNames=MXAN_1925;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2464581; DOI=10.1128/jb.171.2.819-830.1989;
RA Stephens K., Hartzell P.L., Kaiser D.;
RT "Gliding motility in Myxococcus xanthus: mgl locus, RNA, and predicted
RT protein products.";
RL J. Bacteriol. 171:819-830(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hartzell P.L., Youderian P.A.;
RT "Identification of genes required for adventurous gliding motility in
RT Myxococcus xanthus with the transposable element mariner.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1938957; DOI=10.1128/jb.173.23.7615-7624.1991;
RA Hartzell P.L., Kaiser D.;
RT "Function of MglA, a 22-kilodalton protein essential for gliding in
RT Myxococcus xanthus.";
RL J. Bacteriol. 173:7615-7624(1991).
RN [5]
RP FUNCTION.
RX PubMed=10198026; DOI=10.1128/jb.181.8.2593-2601.1999;
RA Spormann A.M., Kaiser D.;
RT "Gliding mutants of Myxococcus xanthus with high reversal frequencies and
RT small displacements.";
RL J. Bacteriol. 181:2593-2601(1999).
RN [6]
RP CHARACTERIZATION.
RX PubMed=12453225; DOI=10.1046/j.1365-2958.2002.03258.x;
RA Thomasson B., Link J., Stassinopoulos A.G., Burke N., Plamann L.,
RA Hartzell P.L.;
RT "MglA, a small GTPase, interacts with a tyrosine kinase to control type IV
RT pili-mediated motility and development of Myxococcus xanthus.";
RL Mol. Microbiol. 46:1399-1413(2002).
RN [7]
RP INTERACTION WITH AGLZ.
RX PubMed=15342587; DOI=10.1128/jb.186.18.6168-6178.2004;
RA Yang R., Bartle S., Otto R., Stassinopoulos A.G., Rogers M., Plamann L.,
RA Hartzell P.L.;
RT "AglZ is a filament-forming coiled-coil protein required for adventurous
RT gliding motility of Myxococcus xanthus.";
RL J. Bacteriol. 186:6168-6178(2004).
CC -!- FUNCTION: Required for multicellular development and for both
CC mechanisms of gliding: social (S) and adventurous (A) motility. Acts as
CC an intracellular switch to coordinate A and S motilities. Controls the
CC direction of gliding and gliding speed. {ECO:0000269|PubMed:10198026,
CC ECO:0000269|PubMed:1938957}.
CC -!- SUBUNIT: Interacts with MasK and AglZ. {ECO:0000269|PubMed:15342587}.
CC -!- INTERACTION:
CC Q1DB04; Q1DB03: mglB; NbExp=2; IntAct=EBI-7643442, EBI-8019001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1938957}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. MglA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF377950; AAA25389.1; -; Genomic_DNA.
DR EMBL; AY197569; AAO66302.1; -; Genomic_DNA.
DR EMBL; CP000113; ABF87984.1; -; Genomic_DNA.
DR PIR; B32048; B32048.
DR RefSeq; WP_011552025.1; NC_008095.1.
DR PDB; 5YMX; X-ray; 1.35 A; A/B=1-195.
DR PDB; 6H17; X-ray; 1.27 A; A=1-195.
DR PDB; 6H35; X-ray; 2.30 A; A/B=1-195.
DR PDB; 6H5B; X-ray; 2.80 A; A=1-195.
DR PDB; 6HJH; X-ray; 3.30 A; A=1-195.
DR PDB; 6HJO; X-ray; 1.98 A; A/B=1-195.
DR PDB; 6IZW; X-ray; 2.40 A; A=1-195.
DR PDBsum; 5YMX; -.
DR PDBsum; 6H17; -.
DR PDBsum; 6H35; -.
DR PDBsum; 6H5B; -.
DR PDBsum; 6HJH; -.
DR PDBsum; 6HJO; -.
DR PDBsum; 6IZW; -.
DR AlphaFoldDB; Q1DB04; -.
DR SMR; Q1DB04; -.
DR IntAct; Q1DB04; 3.
DR MINT; Q1DB04; -.
DR STRING; 246197.MXAN_1925; -.
DR EnsemblBacteria; ABF87984; ABF87984; MXAN_1925.
DR GeneID; 41359339; -.
DR KEGG; mxa:MXAN_1925; -.
DR eggNOG; COG1100; Bacteria.
DR HOGENOM; CLU_077110_0_0_7; -.
DR OMA; MSTINFA; -.
DR OrthoDB; 1438064at2; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0032880; P:regulation of protein localization; IMP:CACAO.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..195
FT /note="Mutual gliding-motility protein MglA"
FT /id="PRO_0000282836"
FT COILED 99..128
FT /evidence="ECO:0000255"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 78..82
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 141..144
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6H17"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:6HJH"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 52..62
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:6H5B"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:6H17"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:6H17"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:6H17"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:6H17"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:6H17"
SQ SEQUENCE 195 AA; 22015 MW; B68657C5110C820E CRC64;
MSFINYSSRE INCKIVYYGP GLCGKTTNLQ YIYNKTAAET KGKLISLSTE TDRTLFFDFL
PLSLGEIRGF KTRFHLYTVP GQVFYDASRK LILKGVDGVV FVADSQIERM EANMESLENL
RINLAEQGYD LNKIPYVIQY NKRDLPNAVT VEEMRKALNH RNIPEYQAVA PTGVGVFDTL
KAVAKLVLTE LKKGG
