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Database: UniProt
Entry: A0A1G1J3P1_9BACT
LinkDB: A0A1G1J3P1_9BACT
Original site: A0A1G1J3P1_9BACT 
ID   A0A1G1J3P1_9BACT        Unreviewed;       323 AA.
AC   A0A1G1J3P1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=A2Z72_00960 {ECO:0000313|EMBL:OGW75275.1};
OS   Omnitrophica bacterium RBG_13_46_9.
OC   Bacteria; Candidatus Omnitrophota.
OX   NCBI_TaxID=1801818 {ECO:0000313|EMBL:OGW75275.1, ECO:0000313|Proteomes:UP000178418};
RN   [1] {ECO:0000313|EMBL:OGW75275.1, ECO:0000313|Proteomes:UP000178418}
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:OGW75275.1}.
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DR   EMBL; MHFD01000053; OGW75275.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G1J3P1; -.
DR   STRING; 1801818.A2Z72_00960; -.
DR   Proteomes; UP000178418; 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   NCBIfam; TIGR01932; hflC; 1.
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; 2.
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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..216
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   323 AA;  36833 MW;  ABA623E8B9328954 CRC64;
     MKQILSLVVA GVIIISALII TGAVYTINET EQVVVTQFGE PMGKPITKAG LHFKIPFIQQ
     ANYFEKRILE WDGNPNQIPT KDKKYIWVDT TARWRIVDAL KFLQSVTTET GAHARLDDIV
     DSATRDFITS HNLVEIVRNT NRIIEERSAE KEKETDGPDQ IAGEIEKIDF GRDTLTRGII
     LEAAKIVPQY GIELIDVRIK RINYVSDVQK KVFERMISER KRAAEQYRSE GQGKKAEIEG
     QMAKELNQIR SEAYKVAEEI KGKADAQAIE IYADAYNRDP DFYSFLKTLD TYRNTIDKDT
     TVILTTNSEY LTYLKDTSQA ARQ
//
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