ID A0A562ZHA3_9BURK Unreviewed; 443 AA.
AC A0A562ZHA3;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:TWO66970.1};
GN ORFNames=FN976_25895 {ECO:0000313|EMBL:TWO66970.1};
OS Caenimonas sedimenti.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Caenimonas.
OX NCBI_TaxID=2596921 {ECO:0000313|EMBL:TWO66970.1, ECO:0000313|Proteomes:UP000318199};
RN [1] {ECO:0000313|EMBL:TWO66970.1, ECO:0000313|Proteomes:UP000318199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HX-9-20 {ECO:0000313|EMBL:TWO66970.1,
RC ECO:0000313|Proteomes:UP000318199};
RA Xu J.;
RT "Caenimonas sedimenti sp. nov., isolated from activated sludge.";
RL Submitted (JUL-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:TWO66970.1}.
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DR EMBL; VOBQ01000024; TWO66970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A562ZHA3; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000318199; 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:TWO66970.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:TWO66970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000318199};
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 24..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 48706 MW; EF1A30A55B35CBF9 CRC64;
MNLPFRGLGF PRLAQRIRGM FNLNDDRWGR GGGDDKKPPE GNKPEGGNNR GQGPNQGPPD
LDELWRDFNR KLGGLFGGRR REGGGGFGGG GGGNFQPDMK SAGVGAGLIA IVVVVIWMGT
GIFIVQEGQQ AVITRFGRYN ATVGAGFNWR LPYPIERHEV VYVTQIRSVD VGRDSVIRTT
GLKESAMLTE DENIVEIKFA VQYRLSDARA WLFESKNPQE AVVQAAETAV REVIGKMRMD
TALAEERDQI GPRVRALMQV ILDRYKVGVE VVGINLQQGG VRPPEQVQAA FDDVLKAGQE
RERAKNEAQA YANDVIPRAR GAASRLQQEA EGYKSRIVSQ AQGDAQRFKS VLTEYQRAPQ
VTRDRMYLDT MQGVYSSVTK IMVESRQGQN MLFLPLDKIM QQVAQGGVAA EPVAPAAAVT
PPPAAAADPR TRDNSRSRER ETR
//
