MOSB_AZOVD
ID MOSB_AZOVD Reviewed; 270 AA.
AC P84253; C1DFP6; Q4IT84;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Molybdenum storage protein subunit beta;
DE Short=Mo storage protein subunit beta;
DE Short=MoSto subunit beta;
GN Name=mosB {ECO:0000303|PubMed:15651045}; OrderedLocusNames=Avin_43210;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-36, IDENTIFICATION, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, MOLYBDENUM-BINDING,
RP AND MASS SPECTROMETRY.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
RX PubMed=15651045; DOI=10.1002/cbic.200400263;
RA Fenske D., Gnida M., Schneider K., Meyer-Klaucke W., Schemberg J.,
RA Henschel V., Meyer A.-K., Knochel A., Muller A.;
RT "A new type of metalloprotein: the Mo storage protein from Azotobacter
RT vinelandii contains a polynuclear molybdenum-oxide cluster.";
RL ChemBioChem 6:405-413(2005).
CC -!- FUNCTION: Intracellular storage of molybdenum. Binds polyoxomolybdates.
CC Can bind at least 90 molybdenum atoms per protein molecule.
CC {ECO:0000269|PubMed:15651045}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 to 7.0. Above pH 7.1 molybdenum is released.
CC {ECO:0000269|PubMed:15651045};
CC -!- SUBUNIT: Octamer consisting of 4 alpha and 4 beta chains.
CC {ECO:0000269|PubMed:15651045}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15651045}.
CC -!- INDUCTION: Requires molybdenum. {ECO:0000269|PubMed:15651045}.
CC -!- MASS SPECTROMETRY: Mass=28150; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15651045};
CC -!- SIMILARITY: Belongs to the UMP kinase family. Highly divergent.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACO80442.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001157; ACO80442.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041807406.1; NC_012560.1.
DR PDB; 2OGX; X-ray; 1.60 A; B=1-270.
DR PDB; 4F6T; X-ray; 1.60 A; B=3-270.
DR PDB; 4NDO; X-ray; 1.35 A; B=1-270.
DR PDB; 4NDP; X-ray; 1.60 A; B=1-270.
DR PDB; 4NDQ; X-ray; 1.75 A; B=1-270.
DR PDB; 4NDR; X-ray; 2.00 A; B=1-270.
DR PDB; 5O5W; X-ray; 1.70 A; B=1-270.
DR PDB; 6GU5; X-ray; 1.90 A; B=2-270.
DR PDB; 6GUJ; X-ray; 2.10 A; B=2-270.
DR PDB; 6GWB; X-ray; 1.90 A; B=2-270.
DR PDB; 6GWV; X-ray; 2.80 A; B/C/E/H/I/K/N/O/Q=2-270.
DR PDB; 6GX4; X-ray; 1.90 A; B=2-270.
DR PDB; 6H6W; X-ray; 1.90 A; B=2-270.
DR PDB; 6H73; X-ray; 2.30 A; B=2-270.
DR PDB; 6H74; X-ray; 1.80 A; B=2-270.
DR PDB; 6H8B; X-ray; 1.90 A; B=2-270.
DR PDB; 6H8H; X-ray; 1.90 A; B=2-270.
DR PDB; 6RIS; X-ray; 2.10 A; B=2-270.
DR PDB; 6RJ4; X-ray; 1.90 A; B/D/F=2-270.
DR PDB; 6RKD; EM; 3.20 A; B/D/F/H/J/L=1-270.
DR PDB; 6RKE; X-ray; 1.70 A; B/D/F/H/J/L=2-270.
DR PDB; 6YT3; X-ray; 2.85 A; B=9-270.
DR PDBsum; 2OGX; -.
DR PDBsum; 4F6T; -.
DR PDBsum; 4NDO; -.
DR PDBsum; 4NDP; -.
DR PDBsum; 4NDQ; -.
DR PDBsum; 4NDR; -.
DR PDBsum; 5O5W; -.
DR PDBsum; 6GU5; -.
DR PDBsum; 6GUJ; -.
DR PDBsum; 6GWB; -.
DR PDBsum; 6GWV; -.
DR PDBsum; 6GX4; -.
DR PDBsum; 6H6W; -.
DR PDBsum; 6H73; -.
DR PDBsum; 6H74; -.
DR PDBsum; 6H8B; -.
DR PDBsum; 6H8H; -.
DR PDBsum; 6RIS; -.
DR PDBsum; 6RJ4; -.
DR PDBsum; 6RKD; -.
DR PDBsum; 6RKE; -.
DR PDBsum; 6YT3; -.
DR AlphaFoldDB; P84253; -.
DR SMR; P84253; -.
DR STRING; 322710.Avin_43210; -.
DR EnsemblBacteria; ACO80442; ACO80442; Avin_43210.
DR KEGG; avn:Avin_43210; -.
DR eggNOG; COG0528; Bacteria.
DR HOGENOM; CLU_1008069_0_0_6; -.
DR OrthoDB; 1043239at2; -.
DR EvolutionaryTrace; P84253; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030151; F:molybdenum ion binding; IDA:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR CDD; cd04255; AAK_UMPK-MosAB; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR030669; MoSto_subunit_alpha/beta.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF039097; MoSto_subunit; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Molybdenum; Storage protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:15651045"
FT CHAIN 2..270
FT /note="Molybdenum storage protein subunit beta"
FT /id="PRO_0000143932"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4NDO"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:4NDO"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 96..118
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:4NDO"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5O5W"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 183..197
FT /evidence="ECO:0007829|PDB:4NDO"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:4NDO"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:4NDO"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:4NDO"
SQ SEQUENCE 270 AA; 28350 MW; 7A7249CC26890E3B CRC64;
MANSTAELEE LLMQRSLTDP QLQAAAAAAA DFRILPDATV IKIGGQSVID RGRAAVYPLV
DEIVAARKNH KLLIGTGAGT RARHLYSIAA GLGLPAGVLA QLGSSVADQN AAMLGQLLAK
HGIPVVGGAG LSAVPLSLAE VNAVVFSGMP PYKLWMRPAA EGVIPPYRTD AGCFLLAEQF
GCKQMIFVKD EDGLYTANPK TSKDATFIPR ISVDEMKAKG LHDSILEFPV LDLLQSAQHV
REVQVVNGLV PGNLTRALAG EHVGTIITAS