ID F9ZP78_ACICS Unreviewed; 387 AA.
AC F9ZP78;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN OrderedLocusNames=Atc_1788 {ECO:0000313|EMBL:AEK58436.1};
OS Acidithiobacillus caldus (strain SM-1).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK58436.1, ECO:0000313|Proteomes:UP000006135};
RN [1] {ECO:0000313|EMBL:AEK58436.1, ECO:0000313|Proteomes:UP000006135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM-1 {ECO:0000313|EMBL:AEK58436.1,
RC ECO:0000313|Proteomes:UP000006135};
RX PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT "Unraveling the Acidithiobacillus caldus complete genome and its central
RT metabolisms for carbon assimilation.";
RL J. Genet. Genomics 38:243-252(2011).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002573; AEK58436.1; -; Genomic_DNA.
DR RefSeq; WP_004872416.1; NC_015850.1.
DR AlphaFoldDB; F9ZP78; -.
DR STRING; 990288.Atc_1788; -.
DR GeneID; 69615321; -.
DR KEGG; acu:Atc_1788; -.
DR HOGENOM; CLU_039173_1_0_6; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000006135; 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 NCBIfam; TIGR01933; hflK; 1.
DR PANTHER; PTHR42911; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR PANTHER; PTHR42911:SF1; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR Pfam; PF01145; Band_7; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 78..248
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 41564 MW; 9F5B5A64B9C18F2A CRC64;
MPWSDPGGNG KQGGNPNPWG RRPGQQQPSW NLTKITSELR KFAGRFGGGR GGPQPFAQHL
RWVPLWVLGG ALVLWLASGV YTLDPQQEGV VLRFGAPVGV VKAGMHYHWP YPIESVAVVN
LQEDRRLVLG YSGAGEQLGP GRMLTADGNV VELRYALRYR VENPEHYLFA AENPNQILAF
ALESAMREAV AQRSLDTLLK GDHSRLAEDV LQATRQRIGA DHLGVKLESV QVLQTALPSD
LDRVAKAVDK ARAQAELERR DAESYAAALL PRAKTEAAAM ISEAQAYRDS AVTRAKGDVA
RFLSLLDVYQ KHPQVIAQQL YLQTMEDILA HAHKVIVGDK QGAIIQITPP TASAAAAPTQ
SGGVVASTTS HGASPEDGAA SNSGGGS
//
