ID A0A3E1RGW1_9BURK Unreviewed; 450 AA.
AC A0A3E1RGW1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:RFO98493.1};
GN ORFNames=DIC66_00970 {ECO:0000313|EMBL:RFO98493.1};
OS Rhodoferax lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO98493.1, ECO:0000313|Proteomes:UP000260665};
RN [1] {ECO:0000313|EMBL:RFO98493.1, ECO:0000313|Proteomes:UP000260665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO98493.1,
RC ECO:0000313|Proteomes:UP000260665};
RA Park M.;
RT "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT lake.";
RL Submitted (MAY-2018) 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}.
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:RFO98493.1}.
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DR EMBL; QFZK01000001; RFO98493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1RGW1; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000260665; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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 SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RFO98493.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:RFO98493.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000260665};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 104..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 120..295
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 49011 MW; C7E15F2819497CD1 CRC64;
MPMQGLKRVF NLNDSRWGRS GEKSDEAGKP ADGTPDSEPP KQPAPDRRPQ NTNSGPPDLD
ELWRDFNRKL GSLFGNKPAG SQGGGTGGAG GNGGFQPDMK TAGVGIGLIL GVLLLIWLGT
GFFIVQEGQQ AVITQFGRYK STVNAGFNWR LPYPIQRHEL VFVTQIRSVD IGRDTVLKAT
GLKESAMLTQ DENILDIKFA VQYRLNDARA FLFESKNPTD AVVQAAETAV REVIGRMRMD
AALSEERDQI APQVRTLMQA ILDRYNVGIE VVGINLQQGG VRPPEQVQAS FDDVLKAGQE
RERAKNEAQA YANDVIPRAV GSASRLKEEA DAYKARVVAQ AQGDAQRFRS VFAEYQKAPQ
VTRDRMYLDT MQQIYTNVTK VVVESKQGSN MLYLPLDKVL QMNGASAGSA DAATSAAAST
TVLPAVPAAN NNASDARARD AARTRDRDVR
//
