ID A0A1B3LPK6_9PROT Unreviewed; 405 AA.
AC A0A1B3LPK6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:AOF82789.1};
GN ORFNames=BSY238_35 {ECO:0000313|EMBL:AOF82789.1};
OS Methyloversatilis sp. RAC08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF82789.1, ECO:0000313|Proteomes:UP000094168};
RN [1] {ECO:0000313|Proteomes:UP000094168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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}.
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DR EMBL; CP016448; AOF82789.1; -; Genomic_DNA.
DR RefSeq; WP_069040343.1; NZ_CP016448.1.
DR AlphaFoldDB; A0A1B3LPK6; -.
DR STRING; 1842540.BSY238_35; -.
DR KEGG; metr:BSY238_35; -.
DR PATRIC; fig|1842540.3.peg.34; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000094168; 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:UP000094168};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 61..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 79..252
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 405 AA; 44573 MW; CCADCD75A78D2743 CRC64;
MSLNDPRWGN QGGNGNKGGN QGPPDLEDLW RDFNKRLAGL FGGKSNNGGG ESRPPVTPRQ
FGSGIGVVLG LIVIVWLASG LYIVDASQRG VVLRFGKLVE TTDPGLQWRL PYPIDSHELV
NLTGVRTVEV GYRGAERNKV LKEALMLTDD ENIINIQFAV QYILKDPVAY LFQNRLPEES
VVHAAETAMR EVVGKSKMDF VLYEGREQIA VDAQRIMQQI LDRYQTGIQI SRLTLQNAQP
PEQVQAAFDD AVKAGQDLER QKNEGQAYAN DVIPKARGTA SRLLEEANGY KERIIATSQG
DASRFKQILA EYVKAPEVTR QRMYIDTVQQ VMMNTSKVLL DAKGGNNLLY LPLDKLMQQA
GAAAVDVAAG SRSNESTTLP SMSGDAAAAD MRSRDALRAR ERGER
//
