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Database: UniProt
Entry: A0A0U2ZEP9_9BACL
LinkDB: A0A0U2ZEP9_9BACL
Original site: A0A0U2ZEP9_9BACL 
ID   A0A0U2ZEP9_9BACL        Unreviewed;       323 AA.
AC   A0A0U2ZEP9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN   ORFNames=AUC31_03435 {ECO:0000313|EMBL:ALS74369.1};
OS   Planococcus rifietoensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS74369.1, ECO:0000313|Proteomes:UP000067683};
RN   [1] {ECO:0000313|EMBL:ALS74369.1, ECO:0000313|Proteomes:UP000067683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8 {ECO:0000313|EMBL:ALS74369.1,
RC   ECO:0000313|Proteomes:UP000067683};
RA   See-Too W.S.;
RT   "Complete genome of Planococcus rifietoensis type strain M8.";
RL   Submitted (JAN-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; CP013659; ALS74369.1; -; Genomic_DNA.
DR   RefSeq; WP_058381076.1; NZ_CP013659.2.
DR   AlphaFoldDB; A0A0U2ZEP9; -.
DR   STRING; 200991.AUC31_03435; -.
DR   KEGG; prt:AUC31_03435; -.
DR   OrthoDB; 9779595at2; -.
DR   Proteomes; UP000067683; 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, ECO:0000256|RuleBase:RU364113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067683};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU364113};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU364113}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364113"
FT   DOMAIN          25..202
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
SQ   SEQUENCE   323 AA;  35875 MW;  C4B23BADD4C354AE CRC64;
     MTTKRVLSII GLSIAGILLL VAVFTSWYTV DESEQAVIIT FGEAGEPVTE SGLHFKMPWP
     IQKAEVMSKE TYSLQFGYDQ NEDGEVTAYD KETKMITGDE NIVLTDLVVQ WKITDPKKFL
     FNAENPREML HDATSASIRS IIGSSLIDDA LTSGKAEIEA ETRDLLSSLI EEYDIGISVL
     AVKLQDVELP NEEVRAAFTN VTDARETMNT KINEANKYEN QKRNEALGEK SAINSRAEAQ
     KVERVEQATG DVAVFDKLYA EYEGNPEVTR QRLIMETLES VLPDAKLYIM NDDEGTMKYL
     PLGEMQTAVP PAAEEQTEEG GGN
//
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