ID   HFLC_BORBU              Reviewed;         323 AA.
AC   O51222;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=Protein HflC;
GN   Name=hflC; OrderedLocusNames=BB_0204;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAC66585.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000783; AAC66585.2; ALT_INIT; Genomic_DNA.
DR   PIR; D70125; D70125.
DR   RefSeq; NP_212338.2; NC_001318.1.
DR   RefSeq; WP_002655940.1; NC_001318.1.
DR   AlphaFoldDB; O51222; -.
DR   SMR; O51222; -.
DR   STRING; 224326.BB_0204; -.
DR   MEROPS; I87.001; -.
DR   PRIDE; O51222; -.
DR   EnsemblBacteria; AAC66585; AAC66585; BB_0204.
DR   KEGG; bbu:BB_0204; -.
DR   PATRIC; fig|224326.49.peg.601; -.
DR   HOGENOM; CLU_059167_1_1_12; -.
DR   OMA; DFFAFYR; -.
DR   Proteomes; UP000001807; 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..323
FT                   /note="Protein HflC"
FT                   /id="PRO_0000094069"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  37194 MW;  18573EB5CBFA7A12 CRC64;
     MKFIINLLLS TIKIITFTVI VCLTILSIFQ PIYILKENEI SITTRLGKIQ RTENLAGLKY
     KIPLIENVQI FPKIILRWDG EPQRIPTGGE EKQLIWIDTT ARWKIADINK FYTTIKTMSR
     AYVRIDAAIE PAVRGVIAKY PLLEIIRSSN DPIQRLSNGI LTPQETKING IYKITKGRKI
     IEKEIIRIAN NNTKDIGIEI VDVLIRKVTY DPSLIESVNN RMISERQQIA EEQRSIGLAE
     KTEILGSIEK EKLKILSEAK ATAAKIKAEG DREAAKIYSN AYGKNIEFYK FWQALESYKA
     VLKDKRKIFS TDMDFFQYLH KRN