OPPA_ECOLI
ID OPPA_ECOLI Reviewed; 543 AA.
AC P23843; P76829;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Periplasmic oligopeptide-binding protein;
DE Flags: Precursor;
GN Name=oppA; OrderedLocusNames=b1243, JW1235;
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=2187863; DOI=10.1016/s0021-9258(19)38898-2;
RA Kashiwagi K., Yamaguchi Y., Sakai Y., Kobayashi H., Igarashi K.;
RT "Identification of the polyamine-induced protein as a periplasmic
RT oligopeptide binding protein.";
RL J. Biol. Chem. 265:8387-8391(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Pahel G., Short S.A.;
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53.
RC STRAIN=K12;
RX PubMed=2015910; DOI=10.1016/0014-5793(91)80358-a;
RA Kessler D., Leibrecht I., Knappe J.;
RT "Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of
RT Escherichia coli reside on a polymeric protein particle encoded by adhE.";
RL FEBS Lett. 281:59-63(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RC STRAIN=DR112;
RA Igarashi K.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 27-37.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S.,
RA Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
RL Submitted (SEP-1994) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 27-38.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP PROTEIN SEQUENCE OF 27-30.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
CC -!- FUNCTION: This protein is a component of the oligopeptide permease, a
CC binding protein-dependent transport system, it binds peptides up to
CC five amino acids long with high affinity.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; J05433; AAA21302.1; -; Genomic_DNA.
DR EMBL; M60918; AAB00918.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74325.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14775.1; -; Genomic_DNA.
DR EMBL; X59501; CAA42089.1; -; Genomic_DNA.
DR EMBL; D83137; BAA11814.1; -; Genomic_DNA.
DR PIR; F64871; F64871.
DR RefSeq; NP_415759.1; NC_000913.3.
DR RefSeq; WP_001393463.1; NZ_CP064683.1.
DR PDB; 3TCF; X-ray; 2.00 A; A/B/C/D/E/F/G/H=27-543.
DR PDB; 3TCG; X-ray; 2.00 A; A/B/C/D/E/F/G/H=27-543.
DR PDB; 3TCH; X-ray; 1.98 A; A=27-543.
DR PDBsum; 3TCF; -.
DR PDBsum; 3TCG; -.
DR PDBsum; 3TCH; -.
DR AlphaFoldDB; P23843; -.
DR SMR; P23843; -.
DR BioGRID; 4263482; 672.
DR BioGRID; 850197; 1.
DR ComplexPortal; CPX-4344; Oligopeptide ABC transporter complex.
DR DIP; DIP-10405N; -.
DR IntAct; P23843; 3.
DR STRING; 511145.b1243; -.
DR TCDB; 3.A.1.5.41; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P23843; -.
DR jPOST; P23843; -.
DR PaxDb; P23843; -.
DR PRIDE; P23843; -.
DR EnsemblBacteria; AAC74325; AAC74325; b1243.
DR EnsemblBacteria; BAA14775; BAA14775; BAA14775.
DR GeneID; 945830; -.
DR KEGG; ecj:JW1235; -.
DR KEGG; eco:b1243; -.
DR PATRIC; fig|511145.12.peg.1293; -.
DR EchoBASE; EB0668; -.
DR eggNOG; COG4166; Bacteria.
DR InParanoid; P23843; -.
DR PhylomeDB; P23843; -.
DR BioCyc; EcoCyc:OPPA-MON; -.
DR BioCyc; MetaCyc:OPPA-MON; -.
DR EvolutionaryTrace; P23843; -.
DR PRO; PR:P23843; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:1900750; F:oligopeptide binding; IDA:EcoCyc.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:EcoCyc.
DR GO; GO:0140205; P:oligopeptide import across plasma membrane; IC:ComplexPortal.
DR GO; GO:0006857; P:oligopeptide transport; IDA:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR023765; SBP_5_CS.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
DR PROSITE; PS01040; SBP_BACTERIAL_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Peptide transport;
KW Periplasm; Protein transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9600841, ECO:0000269|Ref.8"
FT CHAIN 27..543
FT /note="Periplasmic oligopeptide-binding protein"
FT /id="PRO_0000031797"
FT DISULFID 297..443
FT /evidence="ECO:0000250"
FT CONFLICT 271
FT /note="N -> Y (in Ref. 2; AAA21302)"
FT /evidence="ECO:0000305"
FT CONFLICT 314..315
FT /note="RV -> LW (in Ref. 2; AAA21302)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..488
FT /note="QR -> HG (in Ref. 2; AAA21302)"
FT /evidence="ECO:0000305"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 82..93
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 255..263
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 290..303
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 325..330
FT /evidence="ECO:0007829|PDB:3TCH"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 363..376
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:3TCF"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 395..412
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 436..443
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:3TCG"
FT HELIX 485..501
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 505..517
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:3TCH"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:3TCH"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:3TCH"
SQ SEQUENCE 543 AA; 60899 MW; BBEF9FEBD42254EF CRC64;
MTNITKRSLV AAGVLAALMA GNVALAADVP AGVTLAEKQT LVRNNGSEVQ SLDPHKIEGV
PESNISRDLF EGLLVSDLDG HPAPGVAESW DNKDAKVWTF HLRKDAKWSD GTPVTAQDFV
YSWQRSVDPN TASPYASYLQ YGHIAGIDEI LEGKKPITDL GVKAIDDHTL EVTLSEPVPY
FYKLLVHPST SPVPKAAIEK FGEKWTQPGN IVTNGAYTLK DWVVNERIVL ERSPTYWNNA
KTVINQVTYL PIASEVTDVN RYRSGEIDMT NNSMPIELFQ KLKKEIPDEV HVDPYLCTYY
YEINNQKPPF NDVRVRTALK LGMDRDIIVN KVKAQGNMPA YGYTPPYTDG AKLTQPEWFG
WSQEKRNEEA KKLLAEAGYT ADKPLTINLL YNTSDLHKKL AIAASSLWKK NIGVNVKLVN
QEWKTFLDTR HQGTFDVARA GWCADYNEPT SFLNTMLSNS SMNTAHYKSP AFDSIMAETL
KVTDEAQRTA LYTKAEQQLD KDSAIVPVYY YVNARLVKPW VGGYTGKDPL DNTYTRNMYI
VKH
