ID   EAEB_ECO27              Reviewed;         321 AA.
AC   Q05129; B7UM92;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Protein EaeB;
GN   Name=eaeB; Synonyms=espB; OrderedLocusNames=E2348C_3934;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=8393004; DOI=10.1128/jb.175.15.4670-4680.1993;
RA   Donnenberg M.S., Yu J., Kaper J.B.;
RT   "A second chromosomal gene necessary for intimate attachment of
RT   enteropathogenic Escherichia coli to epithelial cells.";
RL   J. Bacteriol. 175:4670-4680(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=9593291; DOI=10.1046/j.1365-2958.1998.00783.x;
RA   Elliott S.J., Wainwright L.A., McDaniel T.K., Jarvis K.G., Deng Y.K.,
RA   Lai L.C., McNamara B.P., Donnenberg M.S., Kaper J.B.;
RT   "The complete sequence of the locus of enterocyte effacement (LEE) from
RT   enteropathogenic Escherichia coli E2348/69.";
RL   Mol. Microbiol. 28:1-4(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Required for the intimate attachment of E.coli to the
CC       epithelial cells. Probable aminotransferase.
CC   -!- INTERACTION:
CC       Q05129; B7UM93: espD; NbExp=2; IntAct=EBI-2530062, EBI-6414369;
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DR   EMBL; Z21555; CAA79733.1; -; Genomic_DNA.
DR   EMBL; AF022236; AAC38396.1; -; Genomic_DNA.
DR   EMBL; FM180568; CAS11482.1; -; Genomic_DNA.
DR   PIR; A40603; A40603.
DR   RefSeq; WP_001091991.1; NC_011601.1.
DR   AlphaFoldDB; Q05129; -.
DR   SMR; Q05129; -.
DR   IntAct; Q05129; 2.
DR   EnsemblBacteria; CAS11482; CAS11482; E2348C_3934.
DR   KEGG; ecg:E2348C_3934; -.
DR   HOGENOM; CLU_905357_0_0_6; -.
DR   OMA; VKSNHDI; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR008611; EaeB.
DR   Pfam; PF05802; EspB; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Cell adhesion; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..321
FT                   /note="Protein EaeB"
FT                   /id="PRO_0000086888"
FT   MOD_RES         139
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   321 AA;  33141 MW;  6D9CF59A0388AA39 CRC64;
     MNTIDNNNAA IAVNSVLSST TDSTSSTTTS TSSISSSLLT DGRVDISKLL LEVQKLLREM
     VTTLQDYLQK QLAQSYDIQK AVFESQNKAI DEKKAGATAA LIGGAISSVL GILGSFAAIN
     SATKGASDVA QQAASTSAKS IGTVSEASTK ALAKASEGIA DAADDAAGAM QQTIATAAKA
     ASRTSGITDD VATSAQKASQ VAEEAADAAQ ELAQKAGLLS RFTAAAGRIS GSTPFIVVTS
     LAEGTKTLPT TISESVKSNH DINEQRAKSV ENLQASNLDT YKQDVRRAQD DISSRLRDMT
     TTARDLTDLI NRMGQAARLA G