ID   MLAC_ECOLI              Reviewed;         211 AA.
AC   P0ADV7; P45390; Q2M920;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Intermembrane phospholipid transport system binding protein MlaC {ECO:0000305};
DE   Flags: Precursor;
GN   Name=mlaC {ECO:0000303|PubMed:19383799}; Synonyms=yrbC;
GN   OrderedLocusNames=b3192, JW3159;
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;
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   [2]
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   [3]
RP   FUNCTION IN PHOSPHOLIPID TRANSPORT, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=K12 / MC4100 / JA176;
RX   PubMed=19383799; DOI=10.1073/pnas.0903229106;
RA   Malinverni J.C., Silhavy T.J.;
RT   "An ABC transport system that maintains lipid asymmetry in the gram-
RT   negative outer membrane.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8009-8014(2009).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 21-210, FUNCTION, AND INTERACTION
RP   WITH MLAFEDB AND MLAA-OMPF.
RC   STRAIN=K12;
RX   PubMed=28388411; DOI=10.1016/j.cell.2017.03.019;
RA   Ekiert D.C., Bhabha G., Isom G.L., Greenan G., Ovchinnikov S.,
RA   Henderson I.R., Cox J.S., Vale R.D.;
RT   "Architectures of lipid transport systems for the bacterial outer
RT   membrane.";
RL   Cell 169:273-285(2017).
CC   -!- FUNCTION: Involved in a phospholipid transport pathway that maintains
CC       lipid asymmetry in the outer membrane by retrograde trafficking of
CC       phospholipids from the outer membrane to the inner membrane. May
CC       transfer phospholipid across the periplasmic space and deliver it to
CC       the MlaFEDB complex at the inner membrane.
CC       {ECO:0000269|PubMed:19383799, ECO:0000305|PubMed:28388411}.
CC   -!- SUBUNIT: Interacts with the MlaA-OmpF outer membrane complex and with
CC       the inner membrane ABC transporter complex MlaFEDB, via direct
CC       interaction with MlaD. {ECO:0000269|PubMed:28388411}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:19383799}.
CC   -!- DISRUPTION PHENOTYPE: Mutation leads to accumulation of phospholipid in
CC       the outer leaflet of the outer membrane and increased outer membrane
CC       permeability. It confers sensitivity to SDS-EDTA.
CC       {ECO:0000269|PubMed:19383799}.
CC   -!- SIMILARITY: Belongs to the MlaC/ttg2D family. {ECO:0000305}.
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DR   EMBL; U18997; AAA57993.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76224.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77236.1; -; Genomic_DNA.
DR   PIR; B65110; B65110.
DR   RefSeq; NP_417659.1; NC_000913.3.
DR   RefSeq; WP_000476487.1; NZ_STEB01000012.1.
DR   PDB; 5UWA; X-ray; 1.50 A; A/B=21-210.
DR   PDB; 6GKI; X-ray; 2.23 A; A/B=22-211.
DR   PDBsum; 5UWA; -.
DR   PDBsum; 6GKI; -.
DR   AlphaFoldDB; P0ADV7; -.
DR   SMR; P0ADV7; -.
DR   BioGRID; 4262983; 22.
DR   IntAct; P0ADV7; 5.
DR   STRING; 511145.b3192; -.
DR   TCDB; 3.A.1.27.3; the atp-binding cassette (abc) superfamily.
DR   SWISS-2DPAGE; P0ADV7; -.
DR   jPOST; P0ADV7; -.
DR   PaxDb; P0ADV7; -.
DR   PRIDE; P0ADV7; -.
DR   EnsemblBacteria; AAC76224; AAC76224; b3192.
DR   EnsemblBacteria; BAE77236; BAE77236; BAE77236.
DR   GeneID; 66672906; -.
DR   GeneID; 947710; -.
DR   KEGG; ecj:JW3159; -.
DR   KEGG; eco:b3192; -.
DR   PATRIC; fig|1411691.4.peg.3539; -.
DR   EchoBASE; EB2650; -.
DR   eggNOG; COG2854; Bacteria.
DR   HOGENOM; CLU_094502_3_0_6; -.
DR   InParanoid; P0ADV7; -.
DR   OMA; ISKSIMT; -.
DR   PhylomeDB; P0ADV7; -.
DR   BioCyc; EcoCyc:G7659-MON; -.
DR   PRO; PR:P0ADV7; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0120010; P:intermembrane phospholipid transfer; IDA:EcoCyc.
DR   GO; GO:0015914; P:phospholipid transport; IMP:EcoCyc.
DR   Gene3D; 3.10.450.710; -; 1.
DR   InterPro; IPR008869; MlaC/ttg2D.
DR   InterPro; IPR042245; Tgt2/MlaC_sf.
DR   PANTHER; PTHR36573; PTHR36573; 1.
DR   Pfam; PF05494; MlaC; 1.
DR   PIRSF; PIRSF004649; MlaC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..211
FT                   /note="Intermembrane phospholipid transport system binding
FT                   protein MlaC"
FT                   /id="PRO_0000013916"
FT   HELIX           27..44
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           55..63
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           70..78
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           87..109
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   STRAND          129..138
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   STRAND          146..154
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   TURN            156..158
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   STRAND          161..168
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           173..180
FT                   /evidence="ECO:0007829|PDB:5UWA"
FT   HELIX           182..201
FT                   /evidence="ECO:0007829|PDB:5UWA"
SQ   SEQUENCE   211 AA;  23963 MW;  A8F22EDFB0830763 CRC64;
     MFKRLMMVAL LVIAPLSAAT AADQTNPYKL MDEAAQKTFD RLKNEQPQIR ANPDYLRTIV
     DQELLPYVQV KYAGALVLGQ YYKSATPAQR EAYFAAFREY LKQAYGQALA MYHGQTYQIA
     PEQPLGDKTI VPIRVTIIDP NGRPPVRLDF QWRKNSQTGN WQAYDMIAEG VSMITTKQNE
     WGTLLRTKGI DGLTAQLKSI SQQKITLEEK K