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Database: UniProt
Entry: A0A0H2V3R1_SHIFL
LinkDB: A0A0H2V3R1_SHIFL
Original site: A0A0H2V3R1_SHIFL 
ID   A0A0H2V3R1_SHIFL        Unreviewed;       419 AA.
AC   A0A0H2V3R1; A0A2G3FB79; Q7BYJ6; Q83P34;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN   Name=hflK {ECO:0000313|EMBL:AAN45746.1};
GN   OrderedLocusNames=SF4329 {ECO:0000313|EMBL:AAN45746.1};
OS   Shigella flexneri.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623 {ECO:0000313|EMBL:AAN45746.1, ECO:0000313|Proteomes:UP000001006};
RN   [1] {ECO:0000313|EMBL:AAN45746.1, ECO:0000313|Proteomes:UP000001006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
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; AE005674; AAN45746.1; -; Genomic_DNA.
DR   RefSeq; NP_710039.1; NC_004337.2.
DR   RefSeq; WP_000312485.1; NZ_WPGW01000048.1.
DR   AlphaFoldDB; A0A0H2V3R1; -.
DR   PaxDb; 198214-SF4329; -.
DR   GeneID; 1025055; -.
DR   KEGG; sfl:SF4329; -.
DR   PATRIC; fig|198214.7.peg.5103; -.
DR   OMA; AWNEPGG; -.
DR   Proteomes; UP000001006; Chromosome.
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   InterPro; IPR001972; Stomatin_HflK_fam.
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   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AAN45746.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW   Protease {ECO:0000313|EMBL:AAN45746.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001006};
KW   Transmembrane {ECO:0000256|RuleBase:RU364113};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364113"
FT   DOMAIN          95..255
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  45531 MW;  E7B271A900869FEC CRC64;
     MAWNQPGNNG QDRDPWGSSK PGGNSEGNGN KGGRDQGPPD LDDIFRKLSK KLGGLGGGKG
     TGSGGGSSSQ GPRPQLGGRV VTIAAAAIVI IWAASGFYTI KEAERGVVTR FGKFSHLVEP
     GLNWKPTFID EVKPVNVEAV RELAASGVML TSDENVVRVE MNVQYRVTNP EKYLYSVTSP
     DDSLRQATDS ALRGVIGKYT MDRILTEGRT VIRSDTQREL EETIRPYDMG ITLLDVNFQA
     ARPPEEVKAA FDDAIAAREN EQQYIREAEA YSNEVQPRAN GQAQRILEEA RAYKAQTILE
     AQGEVARFAK LLPEYKAAPE ITRERLYIET MEKVLGNTRK VLVNDKGGNL MVLPLDQMLK
     GGNAPAAKSD NGASNLLRLP PASSSTTSGA SNTSSTSQGD IMDQRRANAQ RNDYQRQGE
//
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