ID A0A167FVX8_9BACL Unreviewed; 354 AA.
AC A0A167FVX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=PNBC_06065 {ECO:0000313|EMBL:OAB76957.1};
OS Paenibacillus crassostreae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1763538 {ECO:0000313|EMBL:OAB76957.1, ECO:0000313|Proteomes:UP000077134};
RN [1] {ECO:0000313|EMBL:OAB76957.1, ECO:0000313|Proteomes:UP000077134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0068 {ECO:0000313|EMBL:OAB76957.1,
RC ECO:0000313|Proteomes:UP000077134};
RA Shin S.-K., Yi H.;
RT "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL Submitted (FEB-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAB76957.1}.
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DR EMBL; LSFN01000005; OAB76957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167FVX8; -.
DR STRING; 1763538.LPB68_18670; -.
DR Proteomes; UP000077134; Unassembled WGS sequence.
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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Reference proteome {ECO:0000313|Proteomes:UP000077134};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 49..225
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 39331 MW; ABF6A774755450F5 CRC64;
MSLSFMNEDQ NGSQSNKGGP KMPDFKPGTV KKWVIGIAVA IIVIFIGSTS FYTVQEQERA
AVLTFGKYTN ETSAGLHFKW PYPIQQVIMV PAELTQRIHI GYRLQGDESI PVDEEAMMIT
GDENIVSADA VVQWKISNIR DYLFNIDDPE QFLRNAASSS IRAVIGSEKL DYAITDGKTV
IQDKVRVKLL ELQTKYNTGI QIIDIKFQDI EPPSGQVAEA FREVTNAREE KNTKINNAVK
YENDLIPKAR GEAQAFLENA EGEKKSRILN AQGDVAQFNA IYTEYKNNPN VTESRLILET
LEKILPNAQI FITNTNSDTV NYLPLNELLR SGSNDSTTST QTPATTAPEG GAVQ
//
