ID A0A1S2DA35_9GAMM Unreviewed; 411 AA.
AC A0A1S2DA35;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=BC443_05355 {ECO:0000313|EMBL:OHY97217.1};
OS Salinicola sp. MIT1003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Salinicola.
OX NCBI_TaxID=1882734 {ECO:0000313|EMBL:OHY97217.1, ECO:0000313|Proteomes:UP000179615};
RN [1] {ECO:0000313|EMBL:OHY97217.1, ECO:0000313|Proteomes:UP000179615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT1003 {ECO:0000313|EMBL:OHY97217.1,
RC ECO:0000313|Proteomes:UP000179615};
RA Biller S.;
RT "Membrane vesicles in seawater: heterogeneous DNA content and implications
RT for viral abundance estimates.";
RL Submitted (JUL-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:OHY97217.1}.
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; MCAP01000060; OHY97217.1; -; Genomic_DNA.
DR RefSeq; WP_071233253.1; NZ_MCAP01000060.1.
DR AlphaFoldDB; A0A1S2DA35; -.
DR STRING; 1882734.BC443_05355; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000179615; 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 InterPro; IPR020980; Membrane_HflK_N.
DR InterPro; IPR001972; Stomatin_HflK_fam.
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 Pfam; PF12221; HflK_N; 1.
DR PRINTS; PR00721; STOMATIN.
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:UP000179615};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 83..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 100..260
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 REGION 364..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 44435 MW; 5260A0351745ADC6 CRC64;
MAWNEPGGGN NQQDPWGGGG GRRPSGNGGN NGGGNQGPPD LDEALKKFQD KINRLLGGRG
KRSGPGGDGS GGSNGGGGKR NPFLLPILVL IVAAVIWAGS GFHLIDQSER GVVFRLGKYT
ETLNPGLHWN PPIIDRVDSV NVTSIRSATQ TDSMLTSDEN IVRVSVSAQY VVSDSHAFLV
NVNEPEMTLQ NAMDSALRQE VGNMHLQEIL TTGRDRLGQR VFERLTAYME AYGTGLRLQT
VNVESTAPPD QVQDAFDDVI RAREERQRSI NQANAYSQAV VLEAKGQKQR LIEEANGYKA
ASVSDAIGQT NRFNSLLSEY RQAPDVTRQR LYLETMSDVL SKTPKALVDL GDGNAVTVLP
LNQMQAGGNS SQSDSSPMSM QQLEQISRQV IDQMNSGSQQ PTRSSSLREG R
//
