HFLC_ECO57
ID HFLC_ECO57 Reviewed; 334 AA.
AC P0ABC5; P25661;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Modulator of FtsH protease HflC;
GN Name=hflC; OrderedLocusNames=Z5782, ECs5151;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG59371.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38574.1; -; Genomic_DNA.
DR PIR; G86113; G86113.
DR PIR; G91272; G91272.
DR RefSeq; NP_313178.1; NC_002695.1.
DR RefSeq; WP_001232412.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ABC5; -.
DR SMR; P0ABC5; -.
DR STRING; 155864.EDL933_5520; -.
DR MEROPS; I87.001; -.
DR EnsemblBacteria; AAG59371; AAG59371; Z5782.
DR EnsemblBacteria; BAB38574; BAB38574; ECs_5151.
DR GeneID; 66671912; -.
DR GeneID; 914054; -.
DR KEGG; ece:Z5782; -.
DR KEGG; ecs:ECs_5151; -.
DR PATRIC; fig|386585.9.peg.5384; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_059167_3_0_6; -.
DR OMA; DFFAFYR; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..334
FT /note="Modulator of FtsH protease HflC"
FT /id="PRO_0000094074"
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
