ID A0A2K9EIS1_9RHOB Unreviewed; 404 AA.
AC A0A2K9EIS1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:AUH34880.1};
GN ORFNames=CUV01_17175 {ECO:0000313|EMBL:AUH34880.1};
OS Paracoccus tegillarcae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1529068 {ECO:0000313|EMBL:AUH34880.1, ECO:0000313|Proteomes:UP000233742};
RN [1] {ECO:0000313|EMBL:AUH34880.1, ECO:0000313|Proteomes:UP000233742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM15 {ECO:0000313|EMBL:AUH34880.1,
RC ECO:0000313|Proteomes:UP000233742};
RA Hurst M.R.H.;
RL Submitted (DEC-2017) 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; CP025408; AUH34880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K9EIS1; -.
DR KEGG; paro:CUV01_17175; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000233742; 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 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 SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AUH34880.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:AUH34880.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000233742}.
FT DOMAIN 111..279
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 271..298
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 43976 MW; 2529C0CF3A10274A CRC64;
MANQGPWGGG GGNNGGDDGD GKRPSNRPWG DQRPPRDPQR PERPGQGGES MPEIDELMKK
GQERLRVLMG GGRGGRPNGG GGGRGQGPNF SLNRSTIGLI GLGLVLVWGF MSFYTVKPEE
RSVEFLFGDA VGVGEPGLNF APWPFVTAEI VQVTGERVTE IGTGTGPMDS GLMLTRDQNI
VDMEYQVVWN INDPAKYLFN LADPRDTIRA VAESAMRDII ARSELAPILN RDRGAIAEDL
QDAVQQTLDV YESGISVVRV NLDRADPPQE VIDAFREVQA AQQERDRLEK EADAYANRVL
AAARGEAASV LEQAEGYRAQ AVNVAEGEAA RFNSVYDEYV KAPDVTRRRM YLETMERVLG
DVDKVILDAG TMQGGSGVVP YLPLDQLRRD RPTDNSTNDS QGDN
//
