VATB_METMA
ID VATB_METMA Reviewed; 460 AA.
AC Q60187;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=V-type ATP synthase beta chain;
DE AltName: Full=V-ATPase subunit B;
GN Name=atpB; Synonyms=ahaB; OrderedLocusNames=MM_0779;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=8702544; DOI=10.1074/jbc.271.31.18843;
RA Wilms R., Freiberg C., Wegerle E., Meier I., Mayer F., Mueller V.;
RT "Subunit structure and organization of the genes of the A1A0 ATPase from
RT the Archaeon Methanosarcina mazei Go1.";
RL J. Biol. Chem. 271:18843-18852(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The archaeal beta chain is a regulatory subunit.
CC -!- ACTIVITY REGULATION: Stimulated by sulfite, ethanol, glycerol,
CC magnesium and zinc ions.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.2.;
CC -!- SUBUNIT: Composed of seven subunits; A, B, C, D, E, F and G.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM30475.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U47274; AAC06376.1; -; Genomic_DNA.
DR EMBL; AE008384; AAM30475.1; ALT_INIT; Genomic_DNA.
DR PIR; T45108; T45108.
DR RefSeq; WP_015411348.1; NC_003901.1.
DR PDB; 2C61; X-ray; 1.50 A; A/B=1-460.
DR PDB; 2RKW; X-ray; 2.81 A; A/B=1-460.
DR PDB; 3B2Q; X-ray; 2.10 A; A/B=1-460.
DR PDB; 3DSR; X-ray; 2.70 A; A/B=1-460.
DR PDB; 3EIU; X-ray; 3.43 A; A/B=1-460.
DR PDB; 3SSA; X-ray; 1.70 A; A/B=1-460.
DR PDB; 3TGW; X-ray; 1.75 A; A/B=1-460.
DR PDB; 3TIV; X-ray; 1.75 A; A/B=1-460.
DR PDBsum; 2C61; -.
DR PDBsum; 2RKW; -.
DR PDBsum; 3B2Q; -.
DR PDBsum; 3DSR; -.
DR PDBsum; 3EIU; -.
DR PDBsum; 3SSA; -.
DR PDBsum; 3TGW; -.
DR PDBsum; 3TIV; -.
DR AlphaFoldDB; Q60187; -.
DR SMR; Q60187; -.
DR STRING; 192952.MM_0779; -.
DR TCDB; 3.A.2.3.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EnsemblBacteria; AAM30475; AAM30475; MM_0779.
DR GeneID; 44085983; -.
DR GeneID; 66137824; -.
DR KEGG; mma:MM_0779; -.
DR PATRIC; fig|192952.21.peg.927; -.
DR eggNOG; arCOG00865; Archaea.
DR HOGENOM; CLU_022916_0_0_2; -.
DR OMA; GFKIKPR; -.
DR EvolutionaryTrace; Q60187; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR005724; ATPase_A1-cplx_bsu.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01041; ATP_syn_B_arch; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Hydrogen ion transport; Ion transport;
KW Reference proteome; Transport.
FT CHAIN 1..460
FT /note="V-type ATP synthase beta chain"
FT /id="PRO_0000144657"
FT CONFLICT 2
FT /note="A -> V (in Ref. 1; AAC06376)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..68
FT /note="ADIVVVQVFEGTGGLDKDCG -> LTLWLSRFSKVLVGLTRTAV (in
FT Ref. 1; AAC06376)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="S -> F (in Ref. 1; AAC06376)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="D -> E (in Ref. 1; AAC06376)"
FT /evidence="ECO:0000305"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3EIU"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3TGW"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3DSR"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2C61"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3DSR"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3TIV"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2RKW"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 187..200
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 217..238
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 249..256
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:2C61"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:2C61"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 330..334
FT /evidence="ECO:0007829|PDB:2C61"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2C61"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 364..388
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 395..410
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 422..433
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:2C61"
FT HELIX 446..452
FT /evidence="ECO:0007829|PDB:2C61"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:3TGW"
SQ SEQUENCE 460 AA; 50282 MW; 3A7E6BD8ECBB5A7F CRC64;
MAKEYKTITQ IAGPLIFVEK TEPVGYNEIV NIKMGDGTVR RGQVLDSSAD IVVVQVFEGT
GGLDKDCGVI FTGETLKLPA SVDLLGRILS GSGEPRDGGP RIVPDQLLDI NGAAMNPYAR
LPPKDFIQTG ISTIDGTNTL VRGQKLPIFS ASGLPHNEIA LQIARQASVP GSESAFAVVF
AAMGITNEEA QYFMSDFEKT GALERAVVFL NLADDPAVER IVTPRMALTA AEYLAYEHGM
HVLVILTDIT NYAEALRQMG AARNEVPGRR GYPGYMYTDL ATLYERAGIV KGAKGSVTQI
PILSMPGDDI THPIPDLSGY ITEGQIVVAR ELHRKGIYPP INVLPSLSRL MNSGIGAGKT
REDHKAVSDQ MYAGYAEGRD LRGLVAIVGK EALSERDTKF LEFADLFEDK FVRQGRNENR
TIEDTLEIGW QILTHLPENQ LGRIDNKYIQ KYHPAHRKAK
