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Database: UniProt
Entry: A0A1N6XAQ4_9FIRM
LinkDB: A0A1N6XAQ4_9FIRM
Original site: A0A1N6XAQ4_9FIRM 
ID   A0A1N6XAQ4_9FIRM        Unreviewed;       464 AA.
AC   A0A1N6XAQ4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=V-type ATP synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00310};
DE   AltName: Full=V-ATPase subunit B {ECO:0000256|HAMAP-Rule:MF_00310};
GN   Name=atpB {ECO:0000256|HAMAP-Rule:MF_00310};
GN   ORFNames=SAMN05421834_11141 {ECO:0000313|EMBL:SIQ99434.1};
OS   Halanaerobium kushneri.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=56779 {ECO:0000313|EMBL:SIQ99434.1, ECO:0000313|Proteomes:UP000185669};
RN   [1] {ECO:0000313|Proteomes:UP000185669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700103 {ECO:0000313|Proteomes:UP000185669};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The V-type beta chain is a regulatory subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00310}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00310}.
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DR   EMBL; FTNC01000011; SIQ99434.1; -; Genomic_DNA.
DR   RefSeq; WP_076545072.1; NZ_FTNC01000011.1.
DR   AlphaFoldDB; A0A1N6XAQ4; -.
DR   STRING; 56779.SAMN05421834_11141; -.
DR   OrthoDB; 9802718at2; -.
DR   Proteomes; UP000185669; Unassembled WGS sequence.
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   CDD; cd18118; ATP-synt_V_A-type_beta_N; 1.
DR   CDD; cd01135; V_A-ATPase_B; 1.
DR   Gene3D; 3.40.50.12240; -; 1.
DR   HAMAP; MF_00310; ATP_synth_B_arch; 1.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
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; V-TYPE PROTON ATPASE SUBUNIT B; 1.
DR   PANTHER; PTHR43389:SF4; V-TYPE PROTON ATPASE SUBUNIT B; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|HAMAP-Rule:MF_00310};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00310};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00310};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00310}.
FT   DOMAIN          11..74
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          132..350
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
SQ   SEQUENCE   464 AA;  52161 MW;  44FCB7ADAE48D7BE CRC64;
     MLKKEYTGLA NINGPLIVVE NVDDVAYDEM VEVTAPDGEV RKGRVLQVGS NRAVVQVFEG
     STGLNINESR VKFLQEPMKI ALSKDILGRV FNGVGEATDD GGQIYSENKY DINSKPMNPY
     SRQYPRNYIQ TGVSAIDGLM TLIRGQKLPI FSGNGLPHNQ LAAQITRQAK LGKEDEKFAI
     VFVAMGIKHD EARYFINSFE ESGVLQNVVM YVNLADDPSV ERIIAPRVAL TAAEYLAFEE
     NMHILVVMTD MTSYSEALRE LSSRRGEVPG RKGYPGYLYS DLASLYERAG MIKGRDGSIT
     QIPILTMPND DITHPIPDLT GYITEGQIVL ERDLFQRDIY PPINILPSLS RLMKDGIGAE
     YTREDHADIS SQLYAAYSHV NEVKSLASVI GEDELSEIDQ KYLEFGSEFE EEFLNQDKNT
     SRNIEKTLSL AWDLVSELPE HELDRLSEEL IDKYYRRKDE NGET
//
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