ECPD_ECO27
ID ECPD_ECO27 Reviewed; 547 AA.
AC B7UJD8;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Fimbria adhesin EcpD;
DE Flags: Precursor;
GN Name=ecpD; OrderedLocusNames=E2348C_0246;
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 [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).
RN [2]
RP INDUCTION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=22797761; DOI=10.1128/jb.00915-12;
RA Martinez-Santos V.I., Medrano-Lopez A., Saldana Z., Giron J.A.,
RA Puente J.L.;
RT "Transcriptional regulation of the ecp operon by EcpR, IHF, and H-NS in
RT attaching and effacing Escherichia coli.";
RL J. Bacteriol. 194:5020-5033(2012).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH ECPA, AND SUBCELLULAR LOCATION.
RC STRAIN=E2348/69 / EPEC;
RX PubMed=22355107; DOI=10.1073/pnas.1106733109;
RA Garnett J.A., Martinez-Santos V.I., Saldana Z., Pape T., Hawthorne W.,
RA Chan J., Simpson P.J., Cota E., Puente J.L., Giron J.A., Matthews S.;
RT "Structural insights into the biogenesis and biofilm formation by the
RT Escherichia coli common pilus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3950-3955(2012).
CC -!- FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common
CC pilus (ECP). ECP is found in both commensal and pathogenic strains and
CC plays a dual role in early-stage biofilm development and host cell
CC recognition. Tip pilus adhesin, which is required for assembly of EcpA
CC into fibers. {ECO:0000269|PubMed:22355107}.
CC -!- SUBUNIT: Forms polymers. Interacts with EcpA.
CC {ECO:0000269|PubMed:22355107}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:22355107}.
CC Note=Polymerized EcpD is normally incorporated within the tip of ECP,
CC but it can also form functional fimbria independent of EcpA.
CC -!- INDUCTION: Negatively regulated by H-NS. Positively regulated by IHF
CC and EcpR. {ECO:0000269|PubMed:22797761}.
CC -!- SIMILARITY: Belongs to the EcpD/MatE family. {ECO:0000305}.
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DR EMBL; FM180568; CAS07794.1; -; Genomic_DNA.
DR RefSeq; WP_001265644.1; NC_011601.1.
DR AlphaFoldDB; B7UJD8; -.
DR EnsemblBacteria; CAS07794; CAS07794; E2348C_0246.
DR KEGG; ecg:E2348C_0246; -.
DR HOGENOM; CLU_039494_0_0_6; -.
DR OMA; NADCQTQ; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Fimbrium; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..547
FT /note="Fimbria adhesin EcpD"
FT /id="PRO_0000429534"
SQ SEQUENCE 547 AA; 59948 MW; DF9554EBCA9C5CF4 CRC64;
MRVNLLIAMI IFALIWPATA LRAAVSKTTW ADAPAREFVF VENNSDDNFF VTPGGALDPR
LTGANRWTGL KYNGSGTIYQ QSLGYIDNGY NTGLYTNWKF DMWLENSPVS SPLTGLRCIN
WYAGCNMTTS LILPQTTDAS GFYGATVTSG GAKWMHGMLS DAFYQYLQQM PVGSSFTMTI
NACQTSVNYD ASSGARCKDQ ASGNWYVRNV THTKAANLRL INTHSLAEVF INSDGVPTLG
EGNADCRTQT IGSRSGLSCK MVNYTLQTNG LSNTSIHIFP AIANSSLASA VGAYDMQFSL
NGSSWKPVSN TAYYYTFNEM KSADSIYVFF SSNFFKQMVN LGISDINTKD LFNFRFQNTT
SPESGWYEFS TSNTLIIKPR DFSISIISDE YTQTPSREGY VASGESALDF GYIVTTSGKT
AADEVLIKVT GPAQVIGGRS YCVFSSDDGK AKVPFPATLS FITRNGATKT YDAGCDDSWR
DMTDALWLTT PWTDISGEVG QMDKTTVKFS IPMDNAISLR TVDDNGWFGE VSASGEIHVQ
ATWRNIN