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Database: UniProt
Entry: A0A1H8EMB1_9RHOB
LinkDB: A0A1H8EMB1_9RHOB
Original site: A0A1H8EMB1_9RHOB 
ID   A0A1H8EMB1_9RHOB        Unreviewed;       337 AA.
AC   A0A1H8EMB1;
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 HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   ORFNames=SAMN04488003_11129 {ECO:0000313|EMBL:SEN20592.1};
OS   Loktanella fryxellensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=245187 {ECO:0000313|EMBL:SEN20592.1, ECO:0000313|Proteomes:UP000199585};
RN   [1] {ECO:0000313|EMBL:SEN20592.1, ECO:0000313|Proteomes:UP000199585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16213 {ECO:0000313|EMBL:SEN20592.1,
RC   ECO:0000313|Proteomes:UP000199585};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOCI01000011; SEN20592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8EMB1; -.
DR   STRING; 245187.SAMN04488003_11129; -.
DR   OrthoDB; 9812991at2; -.
DR   Proteomes; UP000199585; 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:SEN20592.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000313|EMBL:SEN20592.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199585};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          20..184
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          290..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   337 AA;  36365 MW;  6C78A633DA20234E CRC64;
     MRKSIVLLPV LLVLLVTGIS SVYIVDERQK ALVLQFGQIV KVQESPGLGF KIPFIQNVVR
     YDDRILSRDL EPLEVTPSDD RRLIVDAFAR YRIADVEQFR QAVGAGGEEI AAQRLDGILR
     TVTRNVLGTV ASNDILSVDR AALMLRIRNG AITQAEALGI EVIDVRLKRT DLPAENLNAT
     YERMMAERQR EAADEIARGN EAAQQTRSAA DRTVVELVSD AQRQAEITRG EADAERNAIF
     AGAFGADPEF FEFYRSMTAY QRFAAQGRSS MVLSPDSEFF DYLGSDVGRD GGAATAAADP
     APAGADAAPA AEPEAQLAPD LAPAPGGAQP DTATASN
//
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