ID K9G8C7_PEND1 Unreviewed; 519 AA.
AC K9G8C7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN ORFNames=PDIP_57580 {ECO:0000313|EMBL:EKV11083.1};
OS Penicillium digitatum (strain Pd1 / CECT 20795) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170230 {ECO:0000313|EMBL:EKV11083.1, ECO:0000313|Proteomes:UP000009886};
RN [1] {ECO:0000313|Proteomes:UP000009886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd1 / CECT 20795 {ECO:0000313|Proteomes:UP000009886};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000256|RuleBase:RU003553}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000256|RuleBase:RU003553};
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. {ECO:0000256|RuleBase:RU003553}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV11083.1}.
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DR EMBL; AKCU01000395; EKV11083.1; -; Genomic_DNA.
DR RefSeq; XP_014532984.1; XM_014677498.1.
DR AlphaFoldDB; K9G8C7; -.
DR GeneID; 26234074; -.
DR KEGG; pdp:PDIP_57580; -.
DR HOGENOM; CLU_022398_0_2_1; -.
DR OrthoDB; 3420200at2759; -.
DR Proteomes; UP000009886; Unassembled WGS sequence.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18110; ATP-synt_F1_beta_C; 1.
DR CDD; cd18115; ATP-synt_F1_beta_N; 1.
DR CDD; cd01133; F1-ATPase_beta_CD; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01347; ATP_synth_beta_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005722; ATP_synth_F1_bsu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01039; atpD; 1.
DR PANTHER; PTHR15184; ATP SYNTHASE; 1.
DR PANTHER; PTHR15184:SF71; ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039072; ATPase_subunit_beta; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 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|ARBA:ARBA00023310,
KW ECO:0000256|RuleBase:RU003553};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003553};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|RuleBase:RU003553};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003553};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 187..370
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 519 AA; 55397 MW; 21550D30778CFCBA CRC64;
MFKSGLARSF GRAAFARTTP VARAFQPIRS NALPALTARF ASSDATLIGK VHQVIGAVVD
VKFSGEKLPA IYNAITTTNN GQKLVLEVAQ HLGENIVRTI AMDGTEGLSR GVIAEDTGAP
ITIPVGPATL GRIINVTGDP IDERGPVKAS KFAPIHADPP AFVDQSTSAE ILVTGIKVVD
LLAPYARGGK IGLFGGAGVG KTVFIQELIN NIAKAHGGYS VFCGVGERTR EGNDLYHEMQ
ETGVIQLEGE SKVALVFGQM NEPPGARARV ALTGLTIAEY FRDEEGQDVL LFIDNIFRFT
QAGSEVSALL GRIPSAVGYQ PTLAVDMGVM QERITTTQKG SITSVQAVYV PADDLTDPAP
ATTFAHLDAT TVLSRGISEL GIYPAVDPLD SKSRMLDPRI IGDEHYNTAT RVQQMLQEYK
SLQDIIAILG MDELSEADKL TVERARKLQR FLSQPFAVAQ VFTGIEGTLV DLKDTIASFK
AIIAGEGDDL PEAAFYMVGD INAARAKGEK ILAELENKA
//
