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Database: UniProt
Entry: A0A369QUK9_9RHOB
LinkDB: A0A369QUK9_9RHOB
Original site: A0A369QUK9_9RHOB 
ID   A0A369QUK9_9RHOB        Unreviewed;       321 AA.
AC   A0A369QUK9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=DLJ49_10930 {ECO:0000313|EMBL:RDC72417.1};
OS   Rhodovulum sp. 12E13.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=2203891 {ECO:0000313|EMBL:RDC72417.1, ECO:0000313|Proteomes:UP000253860};
RN   [1] {ECO:0000313|EMBL:RDC72417.1, ECO:0000313|Proteomes:UP000253860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12E13 {ECO:0000313|EMBL:RDC72417.1,
RC   ECO:0000313|Proteomes:UP000253860};
RA   Zhang R.;
RT   "Rhodovulum sp. nov.,isolated from saltern sediment.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: HflC and HflK could regulate a protease.
CC       {ECO:0000256|PIRNR:PIRNR005651}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC       {ECO:0000256|ARBA:ARBA00007862, ECO:0000256|PIRNR:PIRNR005651}.
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:RDC72417.1}.
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DR   EMBL; QPLK01000010; RDC72417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369QUK9; -.
DR   OrthoDB; 9812991at2; -.
DR   Proteomes; UP000253860; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd03405; SPFH_HflC; 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; IPR010200; HflC.
DR   PANTHER; PTHR42911; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR   PANTHER; PTHR42911:SF1; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PIRSF; PIRSF005651; HflC; 1.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:RDC72417.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:RDC72417.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253860};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..186
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          295..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   321 AA;  35336 MW;  A4077232CC720E8D CRC64;
     MKKLGFLIPI LVVAIVGFLS SIFVVDEREK ALVLQFGQIK RVKEDPGLAF KLPVIQEVVR
     YDDRILSLDT QPTEVTPSDD RRLVVDAFAR YRINDVVQFR QAVGVGGLRA AEQRLEGIIN
     PQIRAVLGNE GVTSNTILSA ERSRLMQEIT DQVRSRALPL GLEVVDVRLK RTNLPSQNLD
     ATFARMRAER EREAADEIAR GEEAAQRVRA QADRTVVELT SDAEREAEVI RGEADAERNA
     IFAQAFGADP EFFEFYRSLS AYERAIQGSN STMVISPDSE FFNYLDSSGV RLGGGAGAAP
     GVTGGPLGQV ETPQAGETRQ E
//
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