ID B8EN63_METSB Unreviewed; 368 AA.
AC B8EN63;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN OrderedLocusNames=Msil_0604 {ECO:0000313|EMBL:ACK49576.1};
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965 {ECO:0000313|EMBL:ACK49576.1, ECO:0000313|Proteomes:UP000002257};
RN [1] {ECO:0000313|EMBL:ACK49576.1, ECO:0000313|Proteomes:UP000002257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2
RC {ECO:0000313|Proteomes:UP000002257};
RX PubMed=20472789; DOI=10.1128/JB.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
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}.
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DR EMBL; CP001280; ACK49576.1; -; Genomic_DNA.
DR RefSeq; WP_012589646.1; NC_011666.1.
DR AlphaFoldDB; B8EN63; -.
DR STRING; 395965.Msil_0604; -.
DR KEGG; msl:Msil_0604; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_039173_0_1_5; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000002257; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Reference proteome {ECO:0000313|Proteomes:UP000002257};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 73..252
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 40462 MW; 51C40BE2D9FB3D89 CRC64;
MPWISDGGGG GSWKPSGPWG QKPSSPQQPD FEDLLRRGQE RIKSWMPGSG GGFTGGRGIL
ALALIGIGVW LLSGFYTVAP SEVGLNKIFG RYTGKTGPGL NYNLPFPIGE VEKLPVTTRS
TINVGFTYRP DMRTSVDLPE ESLMLTGDEN IADVKFVVIW QIDPVRPEDY AFNIANQKET
VKAVAESAMR EVIGRSQIQR ILTAERKVIE PAVQELMQRI LNQYKAGVLV LQVQLQSVDP
PEQVIAAFRD VTAAQQDQNR MRNEAEAYAN RVVPEARGKA AATIQEAEGY RLQTVAEATG
QAARFDKIYD EYKKAPGVTR ERMYLETMER VFGGMDKVIV DQDGDRSGVV PYLPLSALTG
KATEGAHK
//
