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Database: UniProt
Entry: A0A1G0XNC6_9BACT
LinkDB: A0A1G0XNC6_9BACT
Original site: A0A1G0XNC6_9BACT 
ID   A0A1G0XNC6_9BACT        Unreviewed;       337 AA.
AC   A0A1G0XNC6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=A2020_15525 {ECO:0000313|EMBL:OGV35093.1};
OS   Lentisphaerae bacterium GWF2_45_14.
OC   Bacteria; Lentisphaerota.
OX   NCBI_TaxID=1798572 {ECO:0000313|EMBL:OGV35093.1, ECO:0000313|Proteomes:UP000176538};
RN   [1] {ECO:0000313|EMBL:OGV35093.1, ECO:0000313|Proteomes:UP000176538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- FUNCTION: HflC and HflK could regulate a protease.
CC       {ECO:0000256|PIRNR:PIRNR005651}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC       {ECO:0000256|ARBA:ARBA00007862, ECO:0000256|PIRNR:PIRNR005651}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGV35093.1}.
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DR   EMBL; MHBG01000063; OGV35093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0XNC6; -.
DR   STRING; 1798572.A2020_15525; -.
DR   Proteomes; UP000176538; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd03405; SPFH_HflC; 1.
DR   Gene3D; 3.30.479.30; Band 7 domain; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR010200; HflC.
DR   PANTHER; PTHR42911; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR   PANTHER; PTHR42911:SF1; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PIRSF; PIRSF005651; HflC; 1.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..210
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          318..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  37760 MW;  03F38D6778902456 CRC64;
     MSSKDSHPPK STRHWGTMFL GLIVAGIFII AVFTYQVKST EWAVVTTLGN ISNLDSQGKF
     IDRGAGLFPK WPYPIQKIVK FDRRNRSFSG NVGKLEETLT NDKKNIIIGI FIVYRITDPV
     QFFKSVITIP NAEEQLNSFM RTSKNAVIGR YRFDQIVNTD SSKVKLSEIE NEIRVQIAAN
     AEKIGIEVGV VGVNSIQLPE KIADKVFNRM ITERQGAAAE YRSQGRKEAE IMKAQADREK
     SQILSGAEAE AKTIRAEGDA KAAEYYSVFR QDPALAAFLR KIDSLRKIMK TKTTLVLDTD
     SAPFDLFKLN ASELEGKVKE LPPKSQPEVR RAPANKK
//
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