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Database: UniProt
Entry: A0A523Q4H5_9BURK
LinkDB: A0A523Q4H5_9BURK
Original site: A0A523Q4H5_9BURK 
ID   A0A523Q4H5_9BURK        Unreviewed;       358 AA.
AC   A0A523Q4H5;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN   Name=hflK {ECO:0000313|EMBL:TDM06370.1};
GN   ORFNames=C4K60_17540 {ECO:0000313|EMBL:TDM06370.1};
OS   Ideonella sp. MAG2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Ideonella.
OX   NCBI_TaxID=2083017 {ECO:0000313|EMBL:TDM06370.1, ECO:0000313|Proteomes:UP000319140};
RN   [1] {ECO:0000313|EMBL:TDM06370.1, ECO:0000313|Proteomes:UP000319140}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAG2 {ECO:0000313|EMBL:TDM06370.1};
RA   Richards S., Han Y., Dugan S., Qu J., Doddapaneni H., Dinh H., Chao H.,
RA   Hughes D., Muzny D., Lee S., Murali S., Worley K., Gibbs R., Poynton H.,
RA   Poelchau M., Werren J., Bowen J., Vineis J.;
RT   "Bacterial draft genomes recovered from genome assembly of Hyalella
RT   azteca.";
RL   Submitted (FEB-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:TDM06370.1}.
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DR   EMBL; PTEU01000002; TDM06370.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A523Q4H5; -.
DR   Proteomes; UP000319140; 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:TDM06370.1};
KW   Membrane {ECO:0000256|RuleBase:RU364113};
KW   Protease {ECO:0000313|EMBL:TDM06370.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000319140};
KW   Transmembrane {ECO:0000256|RuleBase:RU364113};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT   TRANSMEM        85..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364113"
FT   DOMAIN          101..274
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   358 AA;  39048 MW;  755D96D8F6282B19 CRC64;
     MHDSSTPNPG VARLNALSQA LTRAWQRGSR AGWRLLNNGR QDGPPDLDEL WRDFRRKLGG
     IFGKGGGQGP AGGPNFEPDM KSAGVGVGLI AGVVALIWAG SGVFIVQEGE QSVITTFGSY
     SRTVDAGLQW RLPYPFQQNE TVKVTQLRSV DVGRQSVAAS TGLRDSSMLT QDENIVDIRF
     TVQYTLKDAR AFLFENRGTD EAVSQASESA VREIVGRSKV DSVLYERRDA IAADLVKSIQ
     AQLDKLNAGV TIKNVNLKNV EVPEQVQAAF DDAFKAGADR DRYKNEGQAY ASDVIPKAQG
     TASRLAEEAQ GYKSRVVARA EGDAQRFLSV YAEYQKAPGV MRDRLRPRQP LIPPVAHE
//
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