MBA1_YEAST
ID MBA1_YEAST Reviewed; 278 AA.
AC P38300; D6VQI0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Inner membrane mitoribosome receptor MBA1, mitochondrial {ECO:0000303|PubMed:25609543};
DE AltName: Full=Multi-copy bypass of AFG3 protein {ECO:0000303|PubMed:8690083};
DE Flags: Precursor;
GN Name=MBA1 {ECO:0000303|PubMed:8690083}; OrderedLocusNames=YBR185C;
GN ORFNames=YBR1307;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7871891; DOI=10.1002/yea.320101116;
RA Demolis N., Jacquet M., Mallet L.;
RT "A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes
RT encoding ribosomal proteins and six putative new genes, one of which
RT encodes a putative transcriptional factor.";
RL Yeast 10:1511-1525(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=8690083; DOI=10.1016/0014-5793(96)00543-1;
RA Rep M., Grivell L.A.;
RT "MBA1 encodes a mitochondrial membrane-associated protein required for
RT biogenesis of the respiratory chain.";
RL FEBS Lett. 388:185-188(1996).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=11381092; DOI=10.1083/jcb.153.5.1085;
RA Preuss M., Leonhard K., Hell K., Stuart R.A., Neupert W., Herrmann J.M.;
RT "Mba1, a novel component of the mitochondrial protein export machinery of
RT the yeast Saccharomyces cerevisiae.";
RL J. Cell Biol. 153:1085-1096(2001).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, BINDING TO MITORIBOSOMES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16601683; DOI=10.1038/sj.emboj.7601070;
RA Ott M., Prestele M., Bauerschmitt H., Funes S., Bonnefoy N., Herrmann J.M.;
RT "Mba1, a membrane-associated ribosome receptor in mitochondria.";
RL EMBO J. 25:1603-1610(2006).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=18727146; DOI=10.1002/yea.1612;
RA Pir P., Kirdar B., Hayes A., Onsan Z.I., Ulgen K.O., Oliver S.G.;
RT "Exometabolic and transcriptional response in relation to phenotype and
RT gene copy number in respiration-related deletion mutants of S.
RT cerevisiae.";
RL Yeast 25:661-672(2008).
RN [10]
RP SUBCELLULAR LOCATION, AND BINDING TO MITORIBOSOMES AND NASCENT CHAINS.
RX PubMed=20404317; DOI=10.1074/jbc.m110.113837;
RA Gruschke S., Grone K., Heublein M., Holz S., Israel L., Imhof A.,
RA Herrmann J.M., Ott M.;
RT "Proteins at the polypeptide tunnel exit of the yeast mitochondrial
RT ribosome.";
RL J. Biol. Chem. 285:19022-19028(2010).
RN [11]
RP BINDING TO MITORIBOSOMES, INTERACTION WITH MDM38, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=20427570; DOI=10.1091/mbc.e10-02-0101;
RA Bauerschmitt H., Mick D.U., Deckers M., Vollmer C., Funes S., Kehrein K.,
RA Ott M., Rehling P., Herrmann J.M.;
RT "Ribosome-binding proteins Mdm38 and Mba1 display overlapping functions for
RT regulation of mitochondrial translation.";
RL Mol. Biol. Cell 21:1937-1944(2010).
RN [12]
RP SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP OXA1.
RX PubMed=25609543; DOI=10.1038/ncomms7019;
RA Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
RT "Organization of the mitochondrial translation machinery studied in situ by
RT cryoelectron tomography.";
RL Nat. Commun. 6:6019-6019(2015).
CC -!- FUNCTION: Mitochondrial inner membrane-associated mitoribosome receptor
CC that spatially aligns the mitoribosome exit tunnel with the membrane
CC insertion machinery and allows cotranslational protein membrane
CC insertion. {ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683,
CC ECO:0000269|PubMed:20427570, ECO:0000269|PubMed:25609543}.
CC -!- SUBUNIT: Interacts with OXA1 and MDM38. Binds to mitoribosomes in order
CC to recruit them to the mitochondrial inner membrane.
CC {ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:20404317,
CC ECO:0000269|PubMed:20427570, ECO:0000269|PubMed:25609543}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683,
CC ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11381092,
CC ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:25609543,
CC ECO:0000269|PubMed:8690083}; Matrix side {ECO:0000269|PubMed:11381092,
CC ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:25609543,
CC ECO:0000269|PubMed:8690083}. Note=Localizes near the mitoribosome exit
CC tunnel. {ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:20404317}.
CC -!- DISRUPTION PHENOTYPE: Leads to a reduced growth rate on non-fermentable
CC carbon sources, which is more pronounced at high temperature
CC (PubMed:8690083, PubMed:18727146). Shows defects in the membrane
CC insertion of nascent chains resulting in the accumulation of the
CC precursor form of subunit 2 of cytochrome oxidase (PubMed:20427570,
CC PubMed:25609543). {ECO:0000269|PubMed:16601683,
CC ECO:0000269|PubMed:18727146, ECO:0000269|PubMed:20427570,
CC ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083}.
CC -!- MISCELLANEOUS: Present with 2720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U02073; AAB60279.1; -; Genomic_DNA.
DR EMBL; Z36054; CAA85146.1; -; Genomic_DNA.
DR EMBL; AY557862; AAS56188.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07300.1; -; Genomic_DNA.
DR PIR; S46057; S46057.
DR RefSeq; NP_009744.3; NM_001178533.3.
DR AlphaFoldDB; P38300; -.
DR SMR; P38300; -.
DR BioGRID; 32883; 244.
DR DIP; DIP-5701N; -.
DR IntAct; P38300; 11.
DR MINT; P38300; -.
DR STRING; 4932.YBR185C; -.
DR MaxQB; P38300; -.
DR PaxDb; P38300; -.
DR PRIDE; P38300; -.
DR EnsemblFungi; YBR185C_mRNA; YBR185C; YBR185C.
DR GeneID; 852483; -.
DR KEGG; sce:YBR185C; -.
DR SGD; S000000389; MBA1.
DR VEuPathDB; FungiDB:YBR185C; -.
DR eggNOG; ENOG502QWPQ; Eukaryota.
DR HOGENOM; CLU_076697_0_0_1; -.
DR InParanoid; P38300; -.
DR OMA; MMIPGRP; -.
DR BioCyc; YEAST:G3O-29128-MON; -.
DR PRO; PR:P38300; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38300; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0097177; F:mitochondrial ribosome binding; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IDA:SGD.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IGI:SGD.
DR GO; GO:0032979; P:protein insertion into mitochondrial inner membrane from matrix; IMP:SGD.
DR InterPro; IPR024621; Mba1.
DR InterPro; IPR012483; Mba1_Saccharomycetales.
DR Pfam; PF07961; MBA1; 1.
DR PIRSF; PIRSF022613; MBA1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..278
FT /note="Inner membrane mitoribosome receptor MBA1,
FT mitochondrial"
FT /id="PRO_0000021656"
SQ SEQUENCE 278 AA; 31811 MW; 28F92B14BF720678 CRC64;
MSVLRSTCLF FPPRSLLISF NKRRLFSTSR LILNKESETT KKKDKSKQQD FNPRHLGVAA
EIFIPSAYKN LPNVFAHPLI VANALIRRLY TFGLNSVQVA LFRFQSGIKP SFLLWKNKAI
ETYINVNTSF AHKNLSDIKG LVSLWVQEAL EARSRQLPGN ATLDWQLIKF NAVPKLVSVQ
PIMIPGMPLE HLQLVYKFDT KQRLIKVNQQ TKKTETLDRD VVDYIAFLCD ATTNDMILMG
SLFESKPNDK LPKSYEDDAK VAIHRMKVNG DIYRLPPS
