ID   HTRE_ECOLI              Reviewed;         865 AA.
AC   P33129; Q2MCG3;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Outer membrane usher protein HtrE;
DE   AltName: Full=Heat shock protein E;
DE   Flags: Precursor;
GN   Name=htrE; OrderedLocusNames=b0139, JW0135;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=K12;
RX   PubMed=8102362; DOI=10.1128/jb.175.16.5009-5021.1993;
RA   Raina S., Missiakas D., Baird L., Kumar S., Georgopoulos C.;
RT   "Identification and transcriptional analysis of the Escherichia coli htrE
RT   operon which is homologous to pap and related pilin operons.";
RL   J. Bacteriol. 175:5009-5021(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA   Fujita N., Mori H., Yura T., Ishihama A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT   4.1 min (110,917-193,643 bp) region.";
RL   Nucleic Acids Res. 22:1637-1639(1994).
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   PROTEIN SEQUENCE OF 30-33.
RA   Raina S.;
RL   Submitted (DEC-1994) to UniProtKB.
RN   [6]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=20345943; DOI=10.1111/j.1462-2920.2010.02202.x;
RA   Korea C.G., Badouraly R., Prevost M.C., Ghigo J.M., Beloin C.;
RT   "Escherichia coli K-12 possesses multiple cryptic but functional chaperone-
RT   usher fimbriae with distinct surface specificities.";
RL   Environ. Microbiol. 12:1957-1977(2010).
CC   -!- FUNCTION: Part of the yadCKLM-htrE-yadVN fimbrial operon. Could
CC       contribute to adhesion to various surfaces in specific environmental
CC       niches. Probably involved in the export and assembly of fimbrial
CC       subunits across the outer membrane. {ECO:0000269|PubMed:20345943}.
CC   -!- INTERACTION:
CC       P33129; P07813: leuS; NbExp=3; IntAct=EBI-550887, EBI-553345;
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- INDUCTION: Repressed by H-NS. Induced by heat shock.
CC       {ECO:0000269|PubMed:20345943, ECO:0000269|PubMed:8102362}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the operon under classical laboratory
CC       conditions does not result in any major effect on E.coli capacity to
CC       form biofilms compared with the wild-type strain.
CC       {ECO:0000269|PubMed:20345943}.
CC   -!- MISCELLANEOUS: The operon is cryptic under classical laboratory
CC       conditions, but is functional when constitutively expressed.
CC       {ECO:0000305|PubMed:20345943}.
CC   -!- SIMILARITY: Belongs to the fimbrial export usher family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA23721.1; Type=Miscellaneous discrepancy; Note=Incorrect in position 61 onward due to a cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; L00680; AAA23721.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U00096; AAC73250.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76043.1; -; Genomic_DNA.
DR   PIR; C64737; C64737.
DR   RefSeq; NP_414681.1; NC_000913.3.
DR   RefSeq; WP_000151605.1; NZ_LN832404.1.
DR   AlphaFoldDB; P33129; -.
DR   SMR; P33129; -.
DR   BioGRID; 4259738; 125.
DR   BioGRID; 849220; 5.
DR   DIP; DIP-9953N; -.
DR   IntAct; P33129; 9.
DR   STRING; 511145.b0139; -.
DR   TCDB; 1.B.11.3.3; the outer membrane fimbrial usher porin (fup) family.
DR   PaxDb; 511145-b0139; -.
DR   EnsemblBacteria; AAC73250; AAC73250; b0139.
DR   GeneID; 944819; -.
DR   KEGG; ecj:JW0135; -.
DR   KEGG; eco:b0139; -.
DR   PATRIC; fig|1411691.4.peg.2142; -.
DR   EchoBASE; EB1915; -.
DR   eggNOG; COG3188; Bacteria.
DR   HOGENOM; CLU_009120_1_0_6; -.
DR   InParanoid; P33129; -.
DR   OMA; RMKNQFT; -.
DR   OrthoDB; 6554712at2; -.
DR   PhylomeDB; P33129; -.
DR   BioCyc; EcoCyc:EG11972-MONOMER; -.
DR   PRO; PR:P33129; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IBA:GO_Central.
DR   GO; GO:0015473; F:fimbrial usher porin activity; ISS:EcoCyc.
DR   GO; GO:0007155; P:cell adhesion; IMP:EcoCyc.
DR   GO; GO:0009297; P:pilus assembly; IBA:GO_Central.
DR   Gene3D; 2.60.40.2070; -; 1.
DR   Gene3D; 2.60.40.3110; -; 1.
DR   Gene3D; 3.10.20.410; -; 1.
DR   Gene3D; 2.60.40.2610; Outer membrane usher protein FimD, plug domain; 1.
DR   InterPro; IPR000015; Fimb_usher.
DR   InterPro; IPR018030; Fimbrial_membr_usher_CS.
DR   InterPro; IPR042186; FimD_plug_dom.
DR   InterPro; IPR025949; PapC-like_C.
DR   InterPro; IPR043142; PapC-like_C_sf.
DR   InterPro; IPR025885; PapC_N.
DR   InterPro; IPR037224; PapC_N_sf.
DR   PANTHER; PTHR30451; OUTER MEMBRANE USHER PROTEIN; 1.
DR   PANTHER; PTHR30451:SF3; OUTER MEMBRANE USHER PROTEIN HTRE-RELATED; 1.
DR   Pfam; PF13953; PapC_C; 1.
DR   Pfam; PF13954; PapC_N; 1.
DR   Pfam; PF00577; Usher; 1.
DR   SUPFAM; SSF141729; FimD N-terminal domain-like; 1.
DR   PROSITE; PS01151; FIMBRIAL_USHER; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Direct protein sequencing; Disulfide bond;
KW   Fimbrium biogenesis; Membrane; Reference proteome; Signal; Stress response;
KW   Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|Ref.5"
FT   CHAIN           30..865
FT                   /note="Outer membrane usher protein HtrE"
FT                   /id="PRO_0000009319"
FT   DISULFID        838..862
FT                   /evidence="ECO:0000255"
FT   CONFLICT        51
FT                   /note="S -> T (in Ref. 1; AAA23721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        810..811
FT                   /note="QG -> HR (in Ref. 1; AAA23721)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        849
FT                   /note="E -> P (in Ref. 1; AAA23721)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   865 AA;  95499 MW;  F1748B551E4A5AAE CRC64;
     MTIEYTKNYH HLTRIATFCA LLYCNTAFSA ELVEYDHTFL MGQNASNIDL SRYSEGNPAI
     PGVYDVSVYV NDQPIINQSI TFVAIEGKKN AQACITLKNL LQFHINSPDI NNEKAVLLAR
     DETLGNCLNL TEIIPQASVR YDVNDQRLDI DVPQAWVMKN YQNYVDPSLW ENGINAAMLS
     YNLNGYHSET PGRKNESIYA AFNGGMNLGA WRLRASGNYN WMTDSGSNYD FKNRYVQRDI
     ASLRSQLILG ESYTTGETFD SVSIRGIRLY SDSRMLPPTL ASFAPIIHGV ANTNAKVTIT
     QGGYKIYETT VPPGAFVIDD LSPSGYGSDL IVTIEESDGS KRTFSQPFSS VVQMLRPGVG
     RWDISGGQVL KDDIQDEPNL FQASYYYGLN NYLTGYTGIQ ITDNNYTAGL LGLGLNTSVG
     AFSFDVTHSN VRIPDDKTYQ GQSYRVSWNK LFEETSTSLN IAAYRYSTQN YLGLNDALTL
     IDEVKHPEQD LEPKSMRNYS RMKNQVTVSI NQPLKFEKKD YGSFYLSGSW SDYWASGQNR
     SNYSIGYSNS TSWGSYSVSA QRSWNEDGDT DDSVYLSFTI PIEKLLGTEQ RTSGFQSIDT
     QISSDFKGNN QLNVSSSGYS DNARVSYSVN TGYTMNKASK DLSYVGGYAS YESPWGTLAG
     SISANSDNSR QVSLSTDGGF VLHSGGLTFS NDSFSDSDTL AVVQAPGAQG ARINYGNSTI
     DRWGYGVTSA LSPYHENRIA LDINDLENDV ELKSTSAVAV PRQGSVVFAD FETVQGQSAI
     MNITRSDGKN IPFAADIYDE QGNVIGNVGQ GGQAFVRGIE QQGNISIKWL EQSKPVSCLA
     HYQQSPEAEK IAQSIILNGI RCQIQ
//