YOJI_ECOLI
ID YOJI_ECOLI Reviewed; 547 AA.
AC P33941; P33942;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ABC transporter ATP-binding/permease protein YojI {ECO:0000305};
GN Name=yojI; Synonyms=yojJ; OrderedLocusNames=b2211, JW2199;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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 FUNCTION IN MICROCIN J25 RESISTANCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=15866933; DOI=10.1128/jb.187.10.3465-3470.2005;
RA Delgado M.A., Vincent P.A., Farias R.N., Salomon R.A.;
RT "YojI of Escherichia coli functions as a microcin J25 efflux pump.";
RL J. Bacteriol. 187:3465-3470(2005).
CC -!- FUNCTION: Mediates resistance to the antibacterial peptide microcin
CC J25, when expressed from a multicopy vector. Functions as an efflux
CC pump for microcin J25, with the help of the outer membrane channel
CC TolC. {ECO:0000269|PubMed:15866933}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Disruption increases sensitivity of cells to
CC microcin J25. {ECO:0000269|PubMed:15866933}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U00008; AAA16403.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75271.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15994.1; -; Genomic_DNA.
DR PIR; A64991; A64991.
DR RefSeq; NP_416715.1; NC_000913.3.
DR RefSeq; WP_000422182.1; NZ_SSZK01000030.1.
DR AlphaFoldDB; P33941; -.
DR SMR; P33941; -.
DR BioGRID; 4261919; 159.
DR IntAct; P33941; 5.
DR STRING; 511145.b2211; -.
DR TCDB; 3.A.1.113.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P33941; -.
DR PaxDb; P33941; -.
DR PRIDE; P33941; -.
DR EnsemblBacteria; AAC75271; AAC75271; b2211.
DR EnsemblBacteria; BAA15994; BAA15994; BAA15994.
DR GeneID; 946705; -.
DR KEGG; ecj:JW2199; -.
DR KEGG; eco:b2211; -.
DR PATRIC; fig|1411691.4.peg.24; -.
DR EchoBASE; EB1997; -.
DR eggNOG; COG4615; Bacteria.
DR HOGENOM; CLU_023671_1_0_6; -.
DR InParanoid; P33941; -.
DR OMA; GWADTAV; -.
DR PhylomeDB; P33941; -.
DR BioCyc; EcoCyc:YOJI-MON; -.
DR PRO; PR:P33941; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISM:EcoCyc.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042884; P:microcin transport; IMP:EcoliWiki.
DR GO; GO:0046677; P:response to antibiotic; IMP:EcoCyc.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR005898; Cyc_pep_transpt.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43553:SF11; PTHR43553:SF11; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01194; cyc_pep_trnsptr; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..547
FT /note="ABC transporter ATP-binding/permease protein YojI"
FT /id="PRO_0000093196"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 15..291
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 323..547
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 547 AA; 61553 MW; 11523935EDFD9EAB CRC64;
MELLVLVWRQ YRWPFISVMA LSLASAALGI GLIAFINQRL IETADTSLLV LPEFLGLLLL
LMAVTLGSQL ALTTLGHHFV YRLRSEFIKR ILDTHVERIE QLGSASLLAG LTSDVRNITI
AFVRLPELVQ GIILTIGSAA YLWMLSGKML LVTAIWMAIT IWGGFVLVAR VYKHMATLRE
TEDKLYTDFQ TVLEGRKELT LNRERAEYVF NNLYIPDAQE YRHHIIRADT FHLSAVNWSN
IMMLGAIGLV FWMANSLGWA DTNVAATYSL TLLFLRTPLL SAVGALPTLL TAQVAFNKLN
KFALAPFKAE FPRPQAFPNW QTLELRNVTF AYQDNAFSVG PINLTIKRGE LLFLIGGNGS
GKSTLAMLLT GLYQPQSGEI LLDGKPVSGE QPEDYRKLFS AVFTDVWLFD QLLGPEGKPA
NPQLVEKWLA QLKMAHKLEL SNGRIVNLKL SKGQKKRVAL LLALAEERDI ILLDEWAADQ
DPHFRREFYQ VLLPLMQEMG KTIFAISHDD HYFIHADRLL EMRNGQLSEL TGEERDAASR
DAVARTA
