ID   HFLC_TREPA              Reviewed;         331 AA.
AC   O83152;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Protein HflC;
GN   Name=hflC; OrderedLocusNames=TP_0114;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC65104.1; -; Genomic_DNA.
DR   PIR; A71365; A71365.
DR   RefSeq; WP_010881563.1; NC_021490.2.
DR   AlphaFoldDB; O83152; -.
DR   SMR; O83152; -.
DR   IntAct; O83152; 1.
DR   STRING; 243276.TPANIC_0114; -.
DR   MEROPS; I87.001; -.
DR   EnsemblBacteria; AAC65104; AAC65104; TP_0114.
DR   GeneID; 57878657; -.
DR   KEGG; tpa:TP_0114; -.
DR   eggNOG; COG0330; Bacteria.
DR   HOGENOM; CLU_059167_3_0_12; -.
DR   OMA; DFFAFYR; -.
DR   OrthoDB; 1714999at2; -.
DR   Proteomes; UP000000811; 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..331
FT                   /note="Protein HflC"
FT                   /id="PRO_0000094078"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   331 AA;  37594 MW;  6D478740B1756542 CRC64;
     MRKRGLQVHA RVRPVLNIGI VVGVLLGGVV LLQPFYLIQE GQVALITQFG EIIKTNNTAG
     LYVRAPFLHH VHKYTAKLLR VDGDPQKIPT KEKQFIEVDT TSRWRIEDVK KFYQSLGTYE
     AAYSRISDII DSSVRDIITV NGLDDVVRST NAINESNHSE QFDVPVSQLA FDRGAEKTAH
     MTIEKGRESL AREISQAAND QLKDFGIVVV DVIFKGIKYS DELQASVFNR MVKERNQIAQ
     MFRSTGEGKK AEWLGKLDNE KRSLLSKAYE EAERIKGEAD ARAAAVYAQS YGKSPEFYGF
     WKSLEVYKKS LPDTEKILST DLEYFKHLYQ H