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Inner membrane mitoribosome receptor MBA1, mitochondrial (Multi-copy bypass of AFG3 protein)

 MBA1_YEAST              Reviewed;         278 AA.
P38300; D6VQI0;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
25-OCT-2017, entry version 132.
RecName: Full=Inner membrane mitoribosome receptor MBA1, mitochondrial {ECO:0000303|PubMed:25609543};
AltName: Full=Multi-copy bypass of AFG3 protein {ECO:0000303|PubMed:8690083};
Flags: Precursor;
Name=MBA1 {ECO:0000303|PubMed:8690083}; OrderedLocusNames=YBR185C;
ORFNames=YBR1307;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7871891; DOI=10.1002/yea.320101116;
Demolis N., Jacquet M., Mallet L.;
"A 12.5 kb fragment of the yeast chromosome II contains two adjacent
genes encoding ribosomal proteins and six putative new genes, one of
which encodes a putative transcriptional factor.";
Yeast 10:1511-1525(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=8690083; DOI=10.1016/0014-5793(96)00543-1;
Rep M., Grivell L.A.;
"MBA1 encodes a mitochondrial membrane-associated protein required for
biogenesis of the respiratory chain.";
FEBS Lett. 388:185-188(1996).
[6]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11381092; DOI=10.1083/jcb.153.5.1085;
Preuss M., Leonhard K., Hell K., Stuart R.A., Neupert W.,
Herrmann J.M.;
"Mba1, a novel component of the mitochondrial protein export machinery
of the yeast Saccharomyces cerevisiae.";
J. Cell Biol. 153:1085-1096(2001).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
SUBCELLULAR LOCATION, FUNCTION, BINDING TO MITORIBOSOMES, AND
DISRUPTION PHENOTYPE.
PubMed=16601683; DOI=10.1038/sj.emboj.7601070;
Ott M., Prestele M., Bauerschmitt H., Funes S., Bonnefoy N.,
Herrmann J.M.;
"Mba1, a membrane-associated ribosome receptor in mitochondria.";
EMBO J. 25:1603-1610(2006).
[9]
DISRUPTION PHENOTYPE.
PubMed=18727146; DOI=10.1002/yea.1612;
Pir P., Kirdar B., Hayes A., Onsan Z.I., Ulgen K.O., Oliver S.G.;
"Exometabolic and transcriptional response in relation to phenotype
and gene copy number in respiration-related deletion mutants of S.
cerevisiae.";
Yeast 25:661-672(2008).
[10]
SUBCELLULAR LOCATION, AND BINDING TO MITORIBOSOMES AND NASCENT CHAINS.
PubMed=20404317; DOI=10.1074/jbc.M110.113837;
Gruschke S., Grone K., Heublein M., Holz S., Israel L., Imhof A.,
Herrmann J.M., Ott M.;
"Proteins at the polypeptide tunnel exit of the yeast mitochondrial
ribosome.";
J. Biol. Chem. 285:19022-19028(2010).
[11]
BINDING TO MITORIBOSOMES, INTERACTION WITH MDM38, DISRUPTION
PHENOTYPE, AND FUNCTION.
PubMed=20427570; DOI=10.1091/mbc.E10-02-0101;
Bauerschmitt H., Mick D.U., Deckers M., Vollmer C., Funes S.,
Kehrein K., Ott M., Rehling P., Herrmann J.M.;
"Ribosome-binding proteins Mdm38 and Mba1 display overlapping
functions for regulation of mitochondrial translation.";
Mol. Biol. Cell 21:1937-1944(2010).
[12]
SUBCELLULAR LOCATION, FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION
WITH OXA1.
PubMed=25609543; DOI=10.1038/ncomms7019;
Pfeffer S., Woellhaf M.W., Herrmann J.M., Forster F.;
"Organization of the mitochondrial translation machinery studied in
situ by cryoelectron tomography.";
Nat. Commun. 6:6019-6019(2015).
-!- FUNCTION: Mitochondrial inner membrane-associated mitoribosome
receptor that spatially aligns the mitoribosome exit tunnel with
the membrane insertion machinery and allows cotranslational
protein membrane insertion. {ECO:0000269|PubMed:11381092,
ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:20427570,
ECO:0000269|PubMed:25609543}.
-!- SUBUNIT: Interacts with OXA1 and MDM38. Binds to mitoribosomes in
order to recruit them to the mitochondrial inner membrane.
{ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:20404317,
ECO:0000269|PubMed:20427570, ECO:0000269|PubMed:25609543}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683,
ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083};
Peripheral membrane protein {ECO:0000269|PubMed:11381092,
ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:25609543,
ECO:0000269|PubMed:8690083}; Matrix side
{ECO:0000269|PubMed:11381092, ECO:0000269|PubMed:16601683,
ECO:0000269|PubMed:25609543, ECO:0000269|PubMed:8690083}.
Note=Localizes near the mitoribosome exit tunnel.
{ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:20404317}.
-!- DISRUPTION PHENOTYPE: Leads to a reduced growth rate on non-
fermentable carbon sources, which is more pronounced at high
temperature (PubMed:8690083, PubMed:18727146). Shows defects in
the membrane insertion of nascent chains resulting in the
accumulation of the precursor form of subunit 2 of cytochrome
oxidase (PubMed:20427570, PubMed:25609543).
{ECO:0000269|PubMed:16601683, ECO:0000269|PubMed:18727146,
ECO:0000269|PubMed:20427570, ECO:0000269|PubMed:25609543,
ECO:0000269|PubMed:8690083}.
-!- MISCELLANEOUS: Present with 2720 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U02073; AAB60279.1; -; Genomic_DNA.
EMBL; Z36054; CAA85146.1; -; Genomic_DNA.
EMBL; AY557862; AAS56188.1; -; Genomic_DNA.
EMBL; BK006936; DAA07300.1; -; Genomic_DNA.
PIR; S46057; S46057.
RefSeq; NP_009744.3; NM_001178533.3.
ProteinModelPortal; P38300; -.
BioGrid; 32883; 205.
DIP; DIP-5701N; -.
IntAct; P38300; 11.
MINT; MINT-498842; -.
STRING; 4932.YBR185C; -.
MaxQB; P38300; -.
PRIDE; P38300; -.
EnsemblFungi; YBR185C; YBR185C; YBR185C.
GeneID; 852483; -.
KEGG; sce:YBR185C; -.
EuPathDB; FungiDB:YBR185C; -.
SGD; S000000389; MBA1.
HOGENOM; HOG000066059; -.
InParanoid; P38300; -.
KO; K17801; -.
OMA; WKNKAIE; -.
OrthoDB; EOG092C4CBX; -.
BioCyc; YEAST:G3O-29128-MONOMER; -.
PRO; PR:P38300; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
GO; GO:0043022; F:ribosome binding; IDA:SGD.
GO; GO:0007007; P:inner mitochondrial membrane organization; IDA:SGD.
GO; GO:0097033; P:mitochondrial respiratory chain complex III biogenesis; IMP:SGD.
GO; GO:0097034; P:mitochondrial respiratory chain complex IV biogenesis; IMP:SGD.
GO; GO:0070131; P:positive regulation of mitochondrial translation; IGI:SGD.
GO; GO:0032979; P:protein insertion into mitochondrial membrane from inner side; IMP:SGD.
InterPro; IPR024621; Mba1.
InterPro; IPR012483; Mba1_Saccharomycetales.
Pfam; PF07961; MBA1; 1.
PIRSF; PIRSF022613; MBA1; 1.
1: Evidence at protein level;
Complete proteome; Membrane; Mitochondrion;
Mitochondrion inner membrane; Reference proteome; Transit peptide.
TRANSIT 1 33 Mitochondrion. {ECO:0000255}.
CHAIN 34 278 Inner membrane mitoribosome receptor
MBA1, mitochondrial.
/FTId=PRO_0000021656.
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


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