YCCA_ECOLI
ID YCCA_ECOLI Reviewed; 219 AA.
AC P0AAC6; P06967;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Modulator of FtsH protease YccA;
GN Name=yccA; OrderedLocusNames=b0970, JW0953;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6376117; DOI=10.1002/j.1460-2075.1984.tb01936.x;
RA Tamura F., Nishimura S., Ohki M.;
RT "The E. coli divE mutation, which differentially inhibits synthesis of
RT certain proteins, is in tRNASer1.";
RL EMBO J. 3:1103-1107(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
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 [5]
RP SUBSTRATE FOR FTSH, INTERACTION WITH FTSH AND HFLKC, MUTAGENESIS OF
RP 5-VAL--THR-12, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / CSH26 / AD16;
RX PubMed=9636708; DOI=10.1006/jmbi.1998.1781;
RA Kihara A., Akiyama Y., Ito K.;
RT "Different pathways for protein degradation by the FtsH/HflKC membrane-
RT embedded protease complex: an implication from the interference by a mutant
RT form of a new substrate protein, YccA.";
RL J. Mol. Biol. 279:175-188(1998).
RN [6]
RP TOPOLOGY, AND MUTAGENESIS OF 1-MET--THR-12.
RC STRAIN=K12 / CSH26 / AD16;
RX PubMed=10357810; DOI=10.1093/emboj/18.11.2970;
RA Kihara A., Akiyama Y., Ito K.;
RT "Dislocation of membrane proteins in FtsH-mediated proteolysis.";
RL EMBO J. 18:2970-2981(1999).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [8]
RP FUNCTION IN MODULATING FTSH ACTIVITY, AND INDUCTION.
RC STRAIN=K12 / MC4100;
RX PubMed=19661432; DOI=10.1126/science.1172221;
RA van Stelten J., Silva F., Belin D., Silhavy T.J.;
RT "Effects of antibiotics and a proto-oncogene homolog on destruction of
RT protein translocator SecY.";
RL Science 325:753-756(2009).
RN [9]
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: Negatively modulates the activity of the FtsH protease for
CC membrane substrates. Overexpression or stabilizing YccA counteracts the
CC FtsH-mediated degradation of SecY when the SecYEG preprotein
CC translocator is jammed. {ECO:0000269|PubMed:19661432}.
CC -!- SUBUNIT: Both wild-type and the yccA11 mutant interact with the
CC FtsH/HflKC complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC Note=There are conflicting results regarding the localization of the C-
CC terminus of this protein: According to a report, the C-terminus
CC localizes in the periplasm (PubMed:10357810). Another report gives the
CC C-terminus in the cytoplasm (PubMed:15919996). We show the periplasmic
CC location. {ECO:0000269|PubMed:10357810, ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Regulated in a Cpx-dependent fashion.
CC {ECO:0000269|PubMed:19661432}.
CC -!- PTM: YccA is processively degraded by FtsH; degradation initiates via
CC the approximately 20 residue N-terminal tail in a sequence non-specific
CC manner. The deletion mutant yccA11 is resistant to FtsH-mediated
CC degradation, probably because it is too short to be degraded by FtsH.
CC -!- DISRUPTION PHENOTYPE: No effect on SecY degradation.
CC {ECO:0000269|PubMed:9636708}.
CC -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X00547; CAA25218.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74056.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35735.1; -; Genomic_DNA.
DR PIR; S07180; S07180.
DR RefSeq; NP_415490.1; NC_000913.3.
DR RefSeq; WP_000375136.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P0AAC6; -.
DR SMR; P0AAC6; -.
DR BioGRID; 4260037; 11.
DR DIP; DIP-47918N; -.
DR IntAct; P0AAC6; 1.
DR STRING; 511145.b0970; -.
DR TCDB; 1.A.14.2.1; the calcium transporter a (cata) (formerly the testis-enhanced gene transfer (tegt) family.
DR PaxDb; P0AAC6; -.
DR PRIDE; P0AAC6; -.
DR DNASU; 946016; -.
DR EnsemblBacteria; AAC74056; AAC74056; b0970.
DR EnsemblBacteria; BAA35735; BAA35735; BAA35735.
DR GeneID; 67414142; -.
DR GeneID; 946016; -.
DR KEGG; ecj:JW0953; -.
DR KEGG; eco:b0970; -.
DR PATRIC; fig|1411691.4.peg.1303; -.
DR EchoBASE; EB1104; -.
DR eggNOG; COG0670; Bacteria.
DR HOGENOM; CLU_058671_2_1_6; -.
DR InParanoid; P0AAC6; -.
DR OMA; MGDVIGM; -.
DR PhylomeDB; P0AAC6; -.
DR BioCyc; EcoCyc:EG11113-MON; -.
DR PRO; PR:P0AAC6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0030162; P:regulation of proteolysis; IMP:EcoCyc.
DR InterPro; IPR006213; Bax_inhbtr1_CS.
DR InterPro; IPR006214; Bax_inhibitor_1-related.
DR PANTHER; PTHR23291; PTHR23291; 1.
DR Pfam; PF01027; Bax1-I; 1.
DR PROSITE; PS01243; BI1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..219
FT /note="Modulator of FtsH protease YccA"
FT /id="PRO_0000179102"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..46
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..104
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..157
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..219
FT /note="Extracellular"
FT MUTAGEN 1..12
FT /note="MDRIVSSSHDRT->MTMITPSLHDRI: Protein is as sensitive
FT to FtsH degradation as the wild-type."
FT /evidence="ECO:0000269|PubMed:10357810"
FT MUTAGEN 5..12
FT /note="Missing: In yccA11; increases the half-life of
FT overexpressed SecY, F(0) ATP synthase subunit a and itself
FT in an HflKC-dependent fashion, but has no effect on
FT degradation of cytosolic substrates sigma-32 or the phage
FT lambda cII protein. Partially dominant over the wild-type
FT allele. This protein interacts with but is not degraded by
FT FtsH."
FT /evidence="ECO:0000269|PubMed:9636708"
SQ SEQUENCE 219 AA; 23363 MW; 4F787B853042ACD8 CRC64;
MDRIVSSSHD RTSLLSTHKV LRNTYFLLSL TLAFSAITAT ASTVLMLPSP GLILTLVGMY
GLMFLTYKTA NKPTGIISAF AFTGFLGYIL GPILNTYLSA GMGDVIAMAL GGTALVFFCC
SAYVLTTRKD MSFLGGMLMA GIVVVLIGMV ANIFLQLPAL HLAISAVFIL ISSGAILFET
SNIIHGGETN YIRATVSLYV SLYNIFVSLL SILGFASRD
