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}.
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; 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
//