ID A0A1I7ISX3_9BURK Unreviewed; 434 AA.
AC A0A1I7ISX3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=SAMN04489707_10197 {ECO:0000313|EMBL:SFU76025.1};
OS Paenacidovorax caeni.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Paenacidovorax.
OX NCBI_TaxID=343013 {ECO:0000313|EMBL:SFU76025.1, ECO:0000313|Proteomes:UP000183656};
RN [1] {ECO:0000313|EMBL:SFU76025.1, ECO:0000313|Proteomes:UP000183656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R-24608 {ECO:0000313|EMBL:SFU76025.1,
RC ECO:0000313|Proteomes:UP000183656};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPBX01000019; SFU76025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7ISX3; -.
DR STRING; 343013.SAMN04489707_10197; -.
DR Proteomes; UP000183656; 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:SFU76025.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:SFU76025.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000183656};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 90..111
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 106..281
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 47263 MW; 5852A40FA694B5DF CRC64;
MLPQRIRGMF NLNDPRWGRG DDKPADDAHR PDDRPPQGRR NPGPGGQPPD LDELWRDLNR
KLSGLFGGGS GGGRGGNGGG FQPDMRNAGI GAGLIAGIAF VIWMGTGIFI VQEGQQAVIT
QFGKYKATVG AGINWRLPYP IQRHELVFVT QIRSADVGRD SVIKSTGLRD SAMLTEDENI
VEIKFAVQYR LNDARAWLFE SKNPADAVVQ AAETAVREVV GKMRMDTALA EERDQIAPRV
RQLMQTILDR YKIGVEVVGI NLQQGGVRPP EQVQAAFDDV LKAGQERERA KNEAQAYAND
VVPRAVGTAS RLGEEAAAYK ARIVAQAQGD GQRFSALLAE YQKAPQVTRD RLYLEAMQQI
YGNVTKVLVE SRQGSNLLYL PLDKIMQGVA QQPSVAAVDG PPAGPSSAPA AAPSGFGNDS
RTRDNSRSRD RELR
//
