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Database: UniProt
Entry: A0A240USF1_9GAMM
LinkDB: A0A240USF1_9GAMM
Original site: A0A240USF1_9GAMM 
ID   A0A240USF1_9GAMM        Unreviewed;       416 AA.
AC   A0A240USF1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN   ORFNames=B9H00_14195 {ECO:0000313|EMBL:ART64066.1};
OS   Kushneria marisflavi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Kushneria.
OX   NCBI_TaxID=157779 {ECO:0000313|EMBL:ART64066.1, ECO:0000313|Proteomes:UP000194457};
RN   [1] {ECO:0000313|EMBL:ART64066.1, ECO:0000313|Proteomes:UP000194457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SW32 {ECO:0000313|EMBL:ART64066.1};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: HflC and HflK could encode or regulate a protease.
CC       {ECO:0000256|RuleBase:RU364113}.
CC   -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex.
CC       {ECO:0000256|RuleBase:RU364113}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364113}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily.
CC       {ECO:0000256|ARBA:ARBA00006971, ECO:0000256|RuleBase:RU364113}.
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DR   EMBL; CP021358; ART64066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A240USF1; -.
DR   KEGG; kma:B9H00_14195; -.
DR   OrthoDB; 9779595at2; -.
DR   Proteomes; UP000194457; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd03404; SPFH_HflK; 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; IPR010201; HflK.
DR   InterPro; IPR020980; Membrane_HflK_N.
DR   InterPro; IPR001972; Stomatin_HflK_fam.
DR   NCBIfam; TIGR01933; hflK; 1.
DR   PANTHER; PTHR43327:SF2; MODULATOR OF FTSH PROTEASE HFLK; 1.
DR   PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   Pfam; PF12221; HflK_N; 1.
DR   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|RuleBase:RU364113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194457};
KW   Transmembrane {ECO:0000256|RuleBase:RU364113};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT   TRANSMEM        83..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364113"
FT   DOMAIN          100..260
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  45518 MW;  D46045DE6E5662C7 CRC64;
     MAWNEPGGGG NNNQQDPWSG GDRRGGNSGG NKNQGGGPPD LDEVIRKLRN KLNGLLGRRQ
     LRSVNSGDDN GGNNQGGGGR SALLLPIVVL IVGAVVWAGS GFHLIDQSER GVVFRFGKYT
     NTIGPGLHWN PPLIDRVDSV NVTRIRSASQ TDSMLTRDEN IVRVSISAQY VVSDPHAFLV
     NVRGPEMTLQ NAMDSALRQE VGNMELQRIL TTGREELAGD IYDRLASYLE AYGTGIRLQT
     VNMESTSPPD QVQDAFDDVI RAREEQQRTI NRANAYRDAI LPEAEGHRQR MIEEAQGYKA
     AVVADAQGDA NRFVSLLGEY QKAPEVTRQR LYLDTMTEIL SNTPKALVDL GEGNDAVTVL
     PLNQMGRSNS NNSSNSDSDQ SGVDARQLEQ LSQQVVEHMR SNQNQNNGRS SLREGR
//
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