ID A0A1Y5U3N5_9RHOB Unreviewed; 383 AA.
AC A0A1Y5U3N5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK_2 {ECO:0000313|EMBL:SLN76062.1};
GN ORFNames=ROA7023_04096 {ECO:0000313|EMBL:SLN76062.1};
OS Roseisalinus antarcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseisalinus.
OX NCBI_TaxID=254357 {ECO:0000313|EMBL:SLN76062.1, ECO:0000313|Proteomes:UP000193900};
RN [1] {ECO:0000313|EMBL:SLN76062.1, ECO:0000313|Proteomes:UP000193900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7023 {ECO:0000313|EMBL:SLN76062.1,
RC ECO:0000313|Proteomes:UP000193900};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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; FWFZ01000039; SLN76062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5U3N5; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000193900; Unassembled WGS sequence.
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:SLN76062.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:SLN76062.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193900}.
FT DOMAIN 99..267
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..308
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 383 AA; 41191 MW; 72959634C2900A2A CRC64;
MAGNNGGPWG GGGGNNGSDD DENDDRRPAP GRRPGEGPQI PEIDDLMNRG REQLRVLMGG
GGGNNGRRPP FGGGGGGPLL TRGTLGLGAL AAVALWLFSS VYTVRPEEQS VELFLGRYSS
IGNPGLNFAP WPFVTAEVLP VTREQTIDIG TGRAGGDAGL MLTGDENIVD IDFQVVWNIS
DPAQYLFNLA NPPLTIEAVA ESAMREIIAQ SQLAPILNRE RGPIADRLKD LIQLTLDGYD
SGVNVVRVNF DKADPPENVI ASFRAVQDAE QERDRLQNVA DAYANRVLAE SRGQAAQLLE
QAEAYRAQVV NEAEGEASRF EAVLGEYINA PEVTRKRLYL ETMEQVLGGT DIILLDEQEN
GSGVVPYLPL DQLRRNETNG GSN
//
