QMCA_ECOLI
ID QMCA_ECOLI Reviewed; 305 AA.
AC P0AA53; P77367; Q2MBT8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein QmcA;
GN Name=qmcA; Synonyms=ybbK; OrderedLocusNames=b0489, JW0478;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP POSSIBLE FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, POSSIBLE INTERACTION
RP WITH FTSH, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=16573693; DOI=10.1111/j.1365-2958.2006.05104.x;
RA Chiba S., Ito K., Akiyama Y.;
RT "The Escherichia coli plasma membrane contains two PHB (prohibitin
RT homology) domain protein complexes of opposite orientations.";
RL Mol. Microbiol. 60:448-457(2006).
RN [5]
RP REVIEW.
RX PubMed=19454621; DOI=10.1093/jb/mvp071;
RA Akiyama Y.;
RT "Quality control of cytoplasmic membrane proteins in Escherichia coli.";
RL J. Biochem. 146:449-454(2009).
CC -!- FUNCTION: Identified as a multi-copy suppressor of an FtsH/HtpX
CC protease double disruption mutant. May play a role in the quality
CC control of integral membrane proteins.
CC -!- SUBUNIT: Forms oligomers. Probably interacts weakly with FtsH.
CC {ECO:0000269|PubMed:16573693}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:16573693}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16573693}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16573693}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}.
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DR EMBL; U82664; AAB40243.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73591.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76268.1; -; Genomic_DNA.
DR PIR; H64779; H64779.
DR RefSeq; NP_415022.1; NC_000913.3.
DR RefSeq; WP_000904502.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P0AA53; -.
DR SMR; P0AA53; -.
DR BioGRID; 4259648; 29.
DR DIP; DIP-48137N; -.
DR IntAct; P0AA53; 3.
DR STRING; 511145.b0489; -.
DR TCDB; 8.A.21.2.2; the stomatin/podocin/band 7/nephrosis,2/spfh (stomatin) family.
DR jPOST; P0AA53; -.
DR PaxDb; P0AA53; -.
DR PRIDE; P0AA53; -.
DR DNASU; 947257; -.
DR EnsemblBacteria; AAC73591; AAC73591; b0489.
DR EnsemblBacteria; BAE76268; BAE76268; BAE76268.
DR GeneID; 66671209; -.
DR GeneID; 947257; -.
DR KEGG; ecj:JW0478; -.
DR KEGG; eco:b0489; -.
DR PATRIC; fig|1411691.4.peg.1787; -.
DR EchoBASE; EB3046; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_024949_2_2_6; -.
DR InParanoid; P0AA53; -.
DR OMA; TQIRAEM; -.
DR PhylomeDB; P0AA53; -.
DR BioCyc; EcoCyc:G6265-MON; -.
DR PRO; PR:P0AA53; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR032435; Band_7_C.
DR InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF16200; Band_7_C; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..305
FT /note="Protein QmcA"
FT /id="PRO_0000094056"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:16573693"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16573693"
SQ SEQUENCE 305 AA; 33743 MW; 0A7800F65790ACC3 CRC64;
MLIFIPILIF VALVIVGAGV KIVPQGYQWT VERFGRYTKT LQPGLSLVVP FMDRIGRKIN
MMEQVLDIPS QEVISKDNAN VTIDAVCFIQ VIDAPRAAYE VSNLELAIIN LTMTNIRTVL
GSMELDEMLS QRDSINSRLL RIVDEATNPW GIKVTRIEIR DVRPPAELIS SMNAQMKAER
TKRAYILEAE GIRQAEILKA EGEKQSQILK AEGERQSAFL QAEARERSAE AEARATKMVS
EAIASGDIQA VNYFVAQKYT EALQQIGSSS NSKVVMMPLE ASSLMGSIAG IAELVKDSAN
KRTQP
