ID   HFLD_ECOLI              Reviewed;         213 AA.
AC   P25746;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=High frequency lysogenization protein HflD;
GN   Name=hflD; Synonyms=ycfC; OrderedLocusNames=b1132, JW5165;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=8969519; DOI=10.1099/13500872-142-11-3219;
RA   Green S.M., Malik T., Giles I.G., Drabble W.T.;
RT   "The purB gene of Escherichia coli K-12 is located in an operon.";
RL   Microbiology 142:3219-3230(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=1729205; DOI=10.1128/jb.174.1.130-136.1992;
RA   He B., Smith J.M., Zalkin H.;
RT   "Escherichia coli purB gene: cloning, nucleotide sequence, and regulation
RT   by purR.";
RL   J. Bacteriol. 174:130-136(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(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   FUNCTION, SUBUNIT, INTERACTION WITH CII, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11278968; DOI=10.1074/jbc.m011699200;
RA   Kihara A., Akiyama Y., Ito K.;
RT   "Revisiting the lysogenization control of bacteriophage lambda.
RT   Identification and characterization of a new host component, HflD.";
RL   J. Biol. Chem. 276:13695-13700(2001).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-213.
RG   Midwest center for structural genomics (MCSG);
RT   "Structure of a hypothetical protein ycfC coded by Escherichia coli
RT   genome.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Negative regulator of phage lambda lysogenization.
CC       Contributes to the degradation of the phage regulatory protein CII.
CC       Acts probably by holding CII on the membrane surface, away from the
CC       target promoters, but close to the FtsH protease.
CC       {ECO:0000269|PubMed:11278968}.
CC   -!- SUBUNIT: Interacts with CII protein from phage lambda.
CC       {ECO:0000269|PubMed:11278968}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11278968}. Cell
CC       inner membrane {ECO:0000269|PubMed:11278968}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:11278968}; Cytoplasmic side
CC       {ECO:0000269|PubMed:11278968}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an increased
CC       lysogenization frequency. {ECO:0000269|PubMed:11278968}.
CC   -!- SIMILARITY: Belongs to the HflD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M74924; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X59307; CAA41995.1; -; Genomic_DNA.
DR   EMBL; M74924; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U00096; AAC74216.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35954.1; -; Genomic_DNA.
DR   PIR; S19211; S19211.
DR   RefSeq; NP_415650.1; NC_000913.3.
DR   RefSeq; WP_001297479.1; NZ_STEB01000016.1.
DR   PDB; 1QZ4; X-ray; 2.00 A; A=2-213.
DR   PDB; 1SDI; X-ray; 1.65 A; A=2-213.
DR   PDBsum; 1QZ4; -.
DR   PDBsum; 1SDI; -.
DR   AlphaFoldDB; P25746; -.
DR   SMR; P25746; -.
DR   BioGRID; 4263130; 20.
DR   STRING; 511145.b1132; -.
DR   jPOST; P25746; -.
DR   PaxDb; 511145-b1132; -.
DR   EnsemblBacteria; AAC74216; AAC74216; b1132.
DR   GeneID; 83576956; -.
DR   GeneID; 945693; -.
DR   KEGG; ecj:JW5165; -.
DR   KEGG; eco:b1132; -.
DR   PATRIC; fig|1411691.4.peg.1134; -.
DR   EchoBASE; EB1321; -.
DR   eggNOG; COG2915; Bacteria.
DR   HOGENOM; CLU_098920_0_0_6; -.
DR   InParanoid; P25746; -.
DR   OMA; RYIISLM; -.
DR   OrthoDB; 9788031at2; -.
DR   PhylomeDB; P25746; -.
DR   BioCyc; EcoCyc:EG11345-MONOMER; -.
DR   EvolutionaryTrace; P25746; -.
DR   PRO; PR:P25746; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0009408; P:response to heat; IEP:EcoliWiki.
DR   Gene3D; 1.10.3890.10; HflD-like; 1.
DR   HAMAP; MF_00695; HflD_protein; 1.
DR   InterPro; IPR007451; HflD.
DR   InterPro; IPR035932; HflD-like_sf.
DR   PANTHER; PTHR38100; HIGH FREQUENCY LYSOGENIZATION PROTEIN HFLD; 1.
DR   PANTHER; PTHR38100:SF1; HIGH FREQUENCY LYSOGENIZATION PROTEIN HFLD; 1.
DR   Pfam; PF04356; DUF489; 1.
DR   SUPFAM; SSF101322; YcfC-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Coiled coil; Cytoplasm;
KW   Membrane; Reference proteome.
FT   CHAIN           1..213
FT                   /note="High frequency lysogenization protein HflD"
FT                   /id="PRO_0000071576"
FT   COILED          79..126
FT                   /evidence="ECO:0000255"
FT   HELIX           5..28
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           33..44
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           63..74
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           81..101
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           105..114
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           128..141
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           161..183
FT                   /evidence="ECO:0007829|PDB:1SDI"
FT   HELIX           188..208
FT                   /evidence="ECO:0007829|PDB:1SDI"
SQ   SEQUENCE   213 AA;  22948 MW;  E26EF9698C3CEE42 CRC64;
     MAKNYYDITL ALAGICQSAR LVQQLAHQGH CDADALHVSL NSIIDMNPSS TLAVFGGSEA
     NLRVGLETLL GVLNASSRQG LNAELTRYTL SLMVLERKLS SAKGALDTLG NRINGLQRQL
     EHFDLQSETL MSAMAAIYVD VISPLGPRIQ VTGSPAVLQS PQVQAKVRAT LLAGIRAAVL
     WHQVGGGRLQ LMFSRNRLTT QAKQILAHLT PEL
//