MIPA_ECOLI
ID MIPA_ECOLI Reviewed; 248 AA.
AC P0A908; O07962; P77486;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=MltA-interacting protein;
DE Flags: Precursor;
GN Name=mipA; Synonyms=yeaF; OrderedLocusNames=b1782, JW1771;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
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 PROTEIN SEQUENCE OF 23-35, AND INTERACTION WITH MLTA AND MRCB/PONB.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=10037771; DOI=10.1074/jbc.274.10.6726;
RA Vollmer W., von Rechenberg M., Hoeltje J.-V.;
RT "Demonstration of molecular interactions between the murein polymerase
RT PBP1B, the lytic transglycosylase MltA, and the scaffolding protein MipA of
RT Escherichia coli.";
RL J. Biol. Chem. 274:6726-6734(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10806384; DOI=10.1046/j.1432-1327.2000.01296.x;
RA Molloy M.P., Herbert B.R., Slade M.B., Rabilloud T., Nouwens A.S.,
RA Williams K.L., Gooley A.A.;
RT "Proteomic analysis of the Escherichia coli outer membrane.";
RL Eur. J. Biochem. 267:2871-2881(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
CC -!- FUNCTION: May serve as a scaffold protein required for the formation of
CC a complex with MrcB/PonB and MltA, this complex could play a role in
CC enlargement and septation of the murein sacculus.
CC -!- SUBUNIT: Forms a trimeric complex with MrcB and MltA in vitro.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:16079137}.
CC -!- SIMILARITY: Belongs to the MipA/OmpV 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; U00096; AAC74852.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15579.1; -; Genomic_DNA.
DR PIR; F64938; F64938.
DR RefSeq; NP_416296.1; NC_000913.3.
DR RefSeq; WP_000163771.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P0A908; -.
DR BioGRID; 4260311; 187.
DR IntAct; P0A908; 4.
DR STRING; 511145.b1782; -.
DR TCDB; 1.B.93.1.2; the mipa-interacting protein (mipa) family.
DR jPOST; P0A908; -.
DR PaxDb; P0A908; -.
DR PRIDE; P0A908; -.
DR EnsemblBacteria; AAC74852; AAC74852; b1782.
DR EnsemblBacteria; BAA15579; BAA15579; BAA15579.
DR GeneID; 58391373; -.
DR GeneID; 946301; -.
DR KEGG; ecj:JW1771; -.
DR KEGG; eco:b1782; -.
DR PATRIC; fig|1411691.4.peg.472; -.
DR EchoBASE; EB3265; -.
DR eggNOG; COG3713; Bacteria.
DR HOGENOM; CLU_063465_3_0_6; -.
DR InParanoid; P0A908; -.
DR OMA; EVKDSPM; -.
DR PhylomeDB; P0A908; -.
DR BioCyc; EcoCyc:G6968-MON; -.
DR BioCyc; MetaCyc:G6968-MON; -.
DR PRO; PR:P0A908; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR InterPro; IPR010583; MipA.
DR PANTHER; PTHR38776; PTHR38776; 1.
DR Pfam; PF06629; MipA; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Direct protein sequencing; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:10037771"
FT CHAIN 23..248
FT /note="MltA-interacting protein"
FT /id="PRO_0000019092"
FT CONFLICT 34
FT /note="V -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27831 MW; 6571B0D7A47A0525 CRC64;
MTKLKLLALG VLIATSAGVA HAEGKFSLGA GVGVVEHPYK DYDTDVYPVP VINYEGDNFW
FRGLGGGYYL WNDATDKLSI TAYWSPLYFK AKDSGDHQMR HLDDRKSTMM AGLSYAHFTQ
YGYLRTTLAG DTLDNSNGIV WDMAWLYRYT NGGLTVTPGI GVQWNSENQN EYYYGVSRKE
SARSGLRGYN PNDSWSPYLE LSASYNFLGD WSVYGTARYT RLSDEVTDSP MVDKSWTGLI
STGITYKF
