VATB_METKA
ID VATB_METKA Reviewed; 990 AA.
AC Q8TUT0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=V-type ATP synthase beta chain;
DE AltName: Full=V-ATPase subunit B;
DE Contains:
DE RecName: Full=Mka AtpB intein;
GN Name=atpB; OrderedLocusNames=MK1673;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(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 -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the VDE intervening region (intein)
CC followed by peptide ligation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AE009439; AAM02886.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TUT0; -.
DR STRING; 190192.MK1673; -.
DR PRIDE; Q8TUT0; -.
DR EnsemblBacteria; AAM02886; AAM02886; MK1673.
DR KEGG; mka:MK1673; -.
DR PATRIC; fig|190192.8.peg.1837; -.
DR HOGENOM; CLU_301612_0_0_2; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 3.10.28.10; -; 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; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022879; V-ATPase_su_B/beta.
DR PANTHER; PTHR43389; PTHR43389; 2.
DR Pfam; PF00006; ATP-synt_ab; 2.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF14528; LAGLIDADG_3; 2.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF55608; SSF55608; 2.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Autocatalytic cleavage; DNA-binding; Endonuclease;
KW Hydrogen ion transport; Hydrolase; Intron homing; Ion transport; Nuclease;
KW Protein splicing; Reference proteome; Transport.
FT CHAIN 1..260
FT /note="V-type ATP synthase beta chain, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002476"
FT CHAIN 261..777
FT /note="Mka AtpB intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002477"
FT CHAIN 778..990
FT /note="V-type ATP synthase beta chain, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002478"
FT DOMAIN 491..614
FT /note="DOD-type homing endonuclease"
SQ SEQUENCE 990 AA; 110354 MW; 7AC6BE8A32B31585 CRC64;
MAEAERPAGK EYTTISEVSG PLMVVEGVEG AKYGEVVEVE TPTGEVRRGQ VLEARRDAAV
VQVFEGTSGL DTTSTKVRFT GETLRIPVST DLLGRILNGR GEPIDGGPEI VPEDELDIHG
APINPAARKY PSDFIQTGIS AIDGMNTLVR GQKLPIFSGS GLPHNELAAQ IARQATVPGE
EEEFAVVFAA MGITHEEAAF FRREFEETGA LDRAVLILNL ADDPSMERII TPRIALTVAE
YLAFENDMHV LVILTDMTNY CFAPGTRVIT ASGDVVEIDE IVERAAETAV DGGLREGSTE
VTVGVTNVRT LAAWDGDLTS NDVVAVEKIE APSRAVRVRT RSGAELVVSE DHKFLVDTED
GPRMVEASEL KSGDELYSVR ELRVSEKVPT YLELLLEAED KFYVHPTEEF EEAVAERYGS
LAEACREKEL PYRAREAKER RYYELSEFAR LATAVIESVD EATEYIDYVT AGGRKRVKFS
SPRPGKEVMY VAGLIASDGS VDTERGFVMF SNTERELLSA FEEIVTEEFG VDASKTENQN
GVTMLRVNSR VLARVFERLA DPKTVLKMPR ELVAAYLAGY VDGDGHLKDG KIVITTADRE
RAGDLQLLLK RLGVPSVLRE RDGAYDVVVT GHDAAELAEE LPLRHPKKAE AAASMSSGRR
SSRFDRVSRR FGRLLREVRR KYGVRASDLG SSSTISQIES GERRATRRLA LEIVERLEEV
VGDVEEVREL RELAEGNYVL DEVVEVETVE YEHEYLYDVT VVPDHTLVVE NGIITSNCEA
LREISAAREE VPGRRGYPGY MYTDLATIYE RAGCIRGRKG SITQMPILTM PHDDITHPIP
DLTGYITEGQ IVLSRDLHRR GIYPPIDVLP SLSRLMDEGI GKGKTREDHP DLSNQLYAAY
AEGRDLRDLV AVVGEEALTE RDRKFLKFAD EFEQRFVKQG RDENRSIEET LDLGWELLAI
LPERELKRVS DELIEKYHPK YRQKKEEQEE
