ID A0A4R6N9B5_9BURK Unreviewed; 417 AA.
AC A0A4R6N9B5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=DFR39_102107 {ECO:0000313|EMBL:TDP11729.1};
OS Roseateles asaccharophilus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=582607 {ECO:0000313|EMBL:TDP11729.1, ECO:0000313|Proteomes:UP000295357};
RN [1] {ECO:0000313|EMBL:TDP11729.1, ECO:0000313|Proteomes:UP000295357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25082 {ECO:0000313|EMBL:TDP11729.1,
RC ECO:0000313|Proteomes:UP000295357};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TDP11729.1}.
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DR EMBL; SNXE01000002; TDP11729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6N9B5; -.
DR Proteomes; UP000295357; 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:TDP11729.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:TDP11729.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295357};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 95..268
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 45..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 45343 MW; 3D7C7622DDB68AE6 CRC64;
MNNTESAARP WRRLAGRLLM SNGRNDGPPD LDELWRDFNR KLSGLFGGKD GGGQPPQGGN
GHNGGGNNNF QPDMKSAGIG AGLIAGVVVL GWLGSGFYIV QEGHQAVVTS FGKYSKTVDA
GFQWRLPYPF QANEIVPFTQ LRSVEVGRNS VVAATGLRDS SMLTLDENIV DIRFTVQYRL
KDAREYLFEN RSPDEAVIQA AESAVREIVG KSKMDSVLYE QRDAIAADLV KSVQVQLDRL
KAGIVIANVN VQNVQAPEQV QAAFDDAFKA GADRERLKNE GQAYANEVIP KAQGTSARLR
EEAEGYKSRV VAQAEGDAQR FKSVLAEYQK APGVTRDRLY IETMQQVYSN VSKVMVESRS
GSNLLYLPLD KLLQQSGSSV TASPPVPAAL PEAAAAPGSN LDVRSRDGLR GRDRDGR
//
