HFLK_VIBPA
ID HFLK_VIBPA Reviewed; 400 AA.
AC P40605;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein HflK;
GN Name=hflK; OrderedLocusNames=VP2815;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BB22;
RA McCarter L.L.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- FUNCTION: HflC and HflK could encode or regulate a protease.
CC {ECO:0000250}.
CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily.
CC {ECO:0000305}.
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DR EMBL; U09005; AAA62186.1; -; Genomic_DNA.
DR EMBL; BA000031; BAC61078.1; -; Genomic_DNA.
DR RefSeq; NP_799194.1; NC_004603.1.
DR RefSeq; WP_005460667.1; NC_004603.1.
DR AlphaFoldDB; P40605; -.
DR SMR; P40605; -.
DR STRING; 223926.28807825; -.
DR EnsemblBacteria; BAC61078; BAC61078; BAC61078.
DR GeneID; 1190365; -.
DR KEGG; vpa:VP2815; -.
DR PATRIC; fig|223926.6.peg.2706; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_039173_1_0_6; -.
DR OMA; WNEPGGN; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR CDD; cd03404; SPFH_HflK; 1.
DR Gene3D; 3.30.479.30; -; 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 InterPro; IPR001972; Stomatin_HflK_HflKC_fam.
DR PANTHER; PTHR43327:SF2; PTHR43327:SF2; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF12221; HflK_N; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; SSF117892; 1.
DR TIGRFAMs; TIGR01933; hflK; 1.
PE 3: Inferred from homology;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..400
FT /note="Protein HflK"
FT /id="PRO_0000094090"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 44237 MW; B94D8363FD81DC84 CRC64;
MAWNEPGNNN GNNGRDNDPW GNNNRGGQRP GGRDQGPPDL DEVFNKLSQK LGGKFGKKGG
GGSSIGGGGG AIGFGVIAII AIAVWIFAGF YTIGEAERGV VLRLGKYDRI VDPGLNWRPR
FIDEYEAVNV QAIRSLRASG LMLTKDENVV TVAMDVQYRV ADPYKYLYRV TNADDSLRQA
TDSALRAVIG DSLMDSILTS GRQQIRQSTQ ETLNQIIDSY DMGLVIVDVN FQSARPPEQV
KDAFDDAIAA REDEERFIRE AEAYKNEILP KATGRAERLK KEAQGYNERV TNEALGQVAQ
FEKLLPEYQA APGVTRDRLY IDAMEEVYTN TSKVLIDSES SGNLLYLPID KLAGQEGQTD
TKRKSKSSST YDHIQLESER TQEETSNTQS RSTGTRQGRY