ID A0A1I0P460_9RHOB Unreviewed; 381 AA.
AC A0A1I0P460;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=SAMN05444851_1322 {ECO:0000313|EMBL:SEW08833.1};
OS Aliiroseovarius sediminilitoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1173584 {ECO:0000313|EMBL:SEW08833.1, ECO:0000313|Proteomes:UP000199650};
RN [1] {ECO:0000313|EMBL:SEW08833.1, ECO:0000313|Proteomes:UP000199650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29439 {ECO:0000313|EMBL:SEW08833.1,
RC ECO:0000313|Proteomes:UP000199650};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOJB01000001; SEW08833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0P460; -.
DR STRING; 1173584.SAMN05444851_1322; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000199650; 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:SEW08833.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:SEW08833.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199650};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 96..261
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 260..302
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 381 AA; 41079 MW; 5990CF89A23FA0BE CRC64;
MASDNGGPWG GGGNRDGSGG RPPSNGGGNR GGKDQPQMPE IEELMKKGQE QLRVLMGGRG
DKGRGGGSGG GTGGPSFGRG SILLVALVAV AVWVFASFYR VDTSEQSVEL LFGERYGVGQ
EGLNFAPWPI VTREIYPVTR ENVINIGDGT NEGLMLTGDE NIVDIDYQVV WNISDLEKFV
FNLAAPENTI RAVSESAMRE IIARSRLSPI LTSDRGIIAQ DLQELIQSTL DGYQSGVNIV
RVNFDKADPP EDVIDSFREV QAAEQTRDTL QKQADAYANR VVAAARGEAA QLLEEAEGYR
ARVVNEAEGE AARFIAVYDE FAKAPDITRK RLYLETIEKV MRSVDKVILD DNVGGEGGVV
PYLPLNELTR KPAQTTDGGA N
//
