ID A0A3P6UZE2_LITSI Unreviewed; 1389 AA.
AC A0A3P6UZE2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ATP synthase subunit beta {ECO:0000256|RuleBase:RU003553};
DE EC=7.1.2.2 {ECO:0000256|RuleBase:RU003553};
GN ORFNames=NLS_LOCUS6276 {ECO:0000313|EMBL:VDK83594.1};
OS Litomosoides sigmodontis (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Litomosoides.
OX NCBI_TaxID=42156 {ECO:0000313|EMBL:VDK83594.1, ECO:0000313|Proteomes:UP000277928};
RN [1] {ECO:0000313|EMBL:VDK83594.1, ECO:0000313|Proteomes:UP000277928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; UYRX01000540; VDK83594.1; -; Genomic_DNA.
DR STRING; 42156.A0A3P6UZE2; -.
DR Proteomes; UP000277928; 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 CDD; cd00116; LRR_RI; 1.
DR Gene3D; 2.40.10.170; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
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; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
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 Pfam; PF13516; LRR_6; 4.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00368; LRR_RI; 12.
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 SUPFAM; SSF52047; RNI-like; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000277928};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1035..1219
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 359..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1389 AA; 151475 MW; 0FB98B4E253C315A CRC64;
MNSVEINGEW TLSFRDEQKK LDNEADAETM ARVIENADVV EVLELRGNTV GVGAGQRLAH
ALEFHPEMKR ALWSDMFTGR LKEEIPPILR SLCGAMIRCG TQLVELDLSD NAFGPIGAEG
LEEFLGSSSA YSLEVLKLNN NGLGAGGKII AKALMRCHAN AQRDGQNFQL KTFVAGRNRL
EDPGAFALAK AFQVLFIKSS LSVAAVWLEV LGSLEEITMY QDGIRTKGIE ALSESFRYNP
NLKIINLSDN TFTVTGARAM AKVIRDLINL EVLNFGDCLC RDKGALAIIA NISLSHHSHL
KEINLSGNEL SPRTIERILD RVSEGLHLKS LVLHTNNMGV QFDEIKSKCD KYSFVDLGEE
SDDQGTLDEE ESDECQELYS EESHSSDSNS DKQMEGGSVR SIVLTPKTVT QELLSQKFAK
VLDLRGNHIS VDACRRIAEV LQEHTLQNMQ SLEEVNLNQN GITAEGMLEL VNSFKSSPKL
KIIILSGNAL EVDGAVAIAK VLSSLRLLEV LDLSSCACHE RGILAVVASL SSSIHLRLRV
LDFSSNALGA DAIQQIVRFF TSGGFHLERL SLHSNNIGHR FSELKEEFSS VQFLDLGSES
NDQSSLTEEI SAVNSLKRES WSGNGARYTG IDNDTVLFIT KPSVAVLDIL LSDIKTVTES
LHDDLYGRTQ EKTAALLCSC CILLSVESSN KQILKGKIIT LTDAILNAAE KVGRRPVSPT
ESICNQLLAF AGAVRSEGPQ SVANISSVIF LLESMIKRGH FQDLHRTIAF SFNKIKQTYP
DRGVEIDQLM QALRHIKAFS TYSLTEEKLL HIVSYVDMSS RILANFSRSA SRLLCNPKAL
RSVASRTCAS SSINVQKRSL IPVKCGKGLH SSASTLATAD VKKAVSTPPR PTVKGSEGRI
VAVIGAVVDV QFDEGLPPIL NGLEVSGRKP RLILEVSQHL GDNVVRTIAM DGTEGLVRGD
KVIDTGDPIK IPVGPETLGR IMNVIGEPID ERGPINSKHF SPIHAEAPEF VDMSVEQEIL
VTGIKVVDLL APYAKGGKIG LFGGAGVGKT VLIMELINNV AKAHGGYSVF AGVGERTREG
NDLYHEMIEG GVIDLKGKNS KVSLVYGQMN EPPGARARVC LTGLTVAEYF RDKEGQDVLL
FIDNIFRFTQ AGSEVSALLG RIPSAVGYQP TLATDMGGMQ ERITTTKKGS ITSVQAIYVP
ADDLTDPAPA TTFAHLDATT VLSRGIAELA IYPAVDPLDS TSRIMDPNIV GQKHYDIARG
VQKILQVIAL NFIKIGLAGY SRLYLERMGE DYKSLQDIIA ILGMDELSEE DKLVVSRARK
IQKFLSQPFQ VAEVFTGHKG KFVTLEETIK GFELILKGEM DRLPEVAFYM QGGIDDVIAK
ADELAKQNI
//
