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Database: UniProt
Entry: A0A257GV90_9BURK
LinkDB: A0A257GV90_9BURK
Original site: A0A257GV90_9BURK 
ID   A0A257GV90_9BURK        Unreviewed;       291 AA.
AC   A0A257GV90;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
DE   Flags: Fragment;
GN   Name=hflK {ECO:0000313|EMBL:OYU42267.1};
GN   ORFNames=CFE44_24960 {ECO:0000313|EMBL:OYU42267.1};
OS   Burkholderiales bacterium PBB4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=2015566 {ECO:0000313|EMBL:OYU42267.1, ECO:0000313|Proteomes:UP000216392};
RN   [1] {ECO:0000313|EMBL:OYU42267.1, ECO:0000313|Proteomes:UP000216392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PBB4 {ECO:0000313|EMBL:OYU42267.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-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}.
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:OYU42267.1}.
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DR   EMBL; NKIJ01001215; OYU42267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257GV90; -.
DR   Proteomes; UP000216392; 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   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   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:OYU42267.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000313|EMBL:OYU42267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216392}.
FT   DOMAIN          1..137
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          259..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OYU42267.1"
SQ   SEQUENCE   291 AA;  31915 MW;  F1ED4C77F359D8BA CRC64;
     ELGFVTQIRS VDVGRDSVIK ATGLRDSAML TADENILDIK FAVQYRLSDA RAFLFESKNP
     EAAVVQAAET SVREVMGNMK MDAALSEERD QIAPRVRTLM QSILDRYKVG VEVVGINLQQ
     GGVRPPEQVQ ASFDDVLKAG QERERAKNEA QAYANDVIPR AVGTASRLKQ EADAYKAKVV
     AQAQGDAERF RSVYAEYQKA PQVTRDRMYL DAMQQIYSNV TKVLVESKQG SSLLYMPLEK
     IMQMGGAAPT SDAANHAAPV VGAASTSPPV TVISNDARSR ESARTRDRES R
//
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