ID   HFLC_ECOL6              Reviewed;         334 AA.
AC   P0ABC4; P25661;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Modulator of FtsH protease HflC;
GN   Name=hflC; OrderedLocusNames=c5259;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: HflC and HflK help govern the stability of phage lambda cII
CC       protein, and thereby control the lysogenization frequency of phage
CC       lambda. HflKC inhibits the SecY-degrading activity of FtsH, possibly
CC       helping quality control of integral membrane proteins (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: HflC and HflK interact to form a complex, originally called
CC       HflA, now called HflKC. HflKC interacts with FtsH; complex formation is
CC       stimulated by ATP, and with YccA (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE014075; AAN83681.1; -; Genomic_DNA.
DR   RefSeq; WP_001232412.1; NC_004431.1.
DR   AlphaFoldDB; P0ABC4; -.
DR   SMR; P0ABC4; -.
DR   STRING; 199310.c5259; -.
DR   MEROPS; I87.001; -.
DR   EnsemblBacteria; AAN83681; AAN83681; c5259.
DR   GeneID; 66671912; -.
DR   KEGG; ecc:c5259; -.
DR   eggNOG; COG0330; Bacteria.
DR   HOGENOM; CLU_059167_3_0_6; -.
DR   OMA; DFFAFYR; -.
DR   BioCyc; ECOL199310:C5259-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0052547; P:regulation of peptidase activity; IEA:InterPro.
DR   CDD; cd03405; SPFH_HflC; 1.
DR   Gene3D; 3.30.479.30; -; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR010200; HflC.
DR   PANTHER; PTHR42911; PTHR42911; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PIRSF; PIRSF005651; HflC; 1.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; SSF117892; 2.
DR   TIGRFAMs; TIGR01932; hflC; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..334
FT                   /note="Modulator of FtsH protease HflC"
FT                   /id="PRO_0000094075"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        24..334
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   334 AA;  37650 MW;  FC2B0AAC65D27946 CRC64;
     MRKSVIAIII IVLVVLYMSV FVVKEGERGI TLRFGKVLRD DDNKPLVYEP GLHFKIPFIE
     TVKMLDARIQ TMDNQADRFV TKEKKDLIVD SYIKWRISDF SRYYLATGGG DISQAEVLLK
     RKFSDRLRSE IGRLDVKDIV TDSRGRLTLE VRDALNSGSA GTEDEVTTPA ADNAIAEAAE
     RVTAETKGKV PVINPNSMAA LGIEVVDVRI KQINLPTEVS EAIYNRMRAE REAVARRHRS
     QGQEEAEKLR ATADYEVTRT LAEAERQGRI MRGEGDAEAA KLFADAFSKD PDFYAFIRSL
     RAYENSFSGN QDVMVMSPDS DFFRYMKTPT SATR