ATPF_MICLC
ID ATPF_MICLC Reviewed; 184 AA.
AC P80285; C5CA74;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP synthase subunit b;
DE AltName: Full=ATP synthase F(0) sector subunit b;
DE AltName: Full=ATPase subunit I;
DE AltName: Full=F-type ATPase subunit b;
DE Short=F-ATPase subunit b;
GN Name=atpF; OrderedLocusNames=Mlut_08140;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [2]
RP PROTEIN SEQUENCE OF 10-34.
RX PubMed=8011668; DOI=10.1016/0005-2728(94)90133-3;
RA Grueber G., Godovac-Zimmermann J., Nawroth T.;
RT "ATP synthesis and hydrolysis of the ATP-synthase from Micrococcus luteus
RT regulated by an inhibitor subunit and membrane energization.";
RL Biochim. Biophys. Acta 1186:43-51(1994).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000305}.
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DR EMBL; CP001628; ACS30343.1; -; Genomic_DNA.
DR RefSeq; WP_010079019.1; NZ_WBMF01000002.1.
DR AlphaFoldDB; P80285; -.
DR SMR; P80285; -.
DR STRING; 465515.Mlut_08140; -.
DR PRIDE; P80285; -.
DR EnsemblBacteria; ACS30343; ACS30343; Mlut_08140.
DR KEGG; mlu:Mlut_08140; -.
DR PATRIC; fig|465515.4.peg.777; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_5_1_11; -.
DR OMA; FAWKPIL; -.
DR OrthoDB; 1999641at2; -.
DR Proteomes; UP000000738; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..184
FT /note="ATP synthase subunit b"
FT /id="PRO_0000193466"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 33
FT /note="L -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 19904 MW; AB93C6DB69F463AC CRC64;
MISNGLILAA AEGANPLIPN PWEILVVVVG FALLMFIVIK FIVPTLEKSY QDRVEAIEGG
LAKAEKAQAE ANAMMADYES QLADARTEAN RIREDARTEA AEIVAEARER ATAEATRVFE
QAQAQIAAER QQAAAQLKRE VGSLATTLAG KIVGESLEDD ARSQRVVDRF LADLDRHQSA
GVAE
