HFLC_BUCBP
ID HFLC_BUCBP Reviewed; 326 AA.
AC Q89A40;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Protein HflC;
GN Name=hflC; OrderedLocusNames=bbp_512;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: HflC and HflK could regulate a protease. {ECO:0000250}.
CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016826; AAO27215.1; -; Genomic_DNA.
DR RefSeq; WP_011091616.1; NC_004545.1.
DR AlphaFoldDB; Q89A40; -.
DR SMR; Q89A40; -.
DR STRING; 224915.bbp_512; -.
DR EnsemblBacteria; AAO27215; AAO27215; bbp_512.
DR GeneID; 56471047; -.
DR KEGG; bab:bbp_512; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_059167_3_0_6; -.
DR OMA; DFFAFYR; -.
DR OrthoDB; 1714999at2; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 1.
DR TIGRFAMs; TIGR01932; hflC; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..326
FT /note="Protein HflC"
FT /id="PRO_0000094072"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 326 AA; 37976 MW; DDF088C60BC5125B CRC64;
MRKVILIILI VVVIYFFTCF FIIKEGQRGI ILRFGKISYD DNHHVLVYKP GLHIKLPFIE
SVKIFNSKIQ TIDNRLDSVL TKDNKNLVLN TYINWKINDF CRYYLSTGED NIYYAETLIK
QKFNNRLRAQ ISHLNIKEII FNVKDQLTSN IKYSLNASSK INYKNVIFKK AINGTSNQNI
NQENNLLQSI SDLSEIGVQI LDVRIGKISV SEDFFSLICS RINSEYRAIA KHYRLMGDKQ
AEELKLRANY EVVKILSKAQ RSALIIKSEG EALVAKLFSD AFSQEPEFFS FIRSLQAYEN
IFKKKNQNLI VVNENNSSFL RYMYIK