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Database: UniProt
Entry: A0A0U1NJG9_9RHOB
LinkDB: A0A0U1NJG9_9RHOB
Original site: A0A0U1NJG9_9RHOB 
ID   A0A0U1NJG9_9RHOB        Unreviewed;       294 AA.
AC   A0A0U1NJG9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN   Name=hflC {ECO:0000313|EMBL:CRK74845.1};
GN   ORFNames=NIG5292_00884 {ECO:0000313|EMBL:CRK74845.1};
OS   Nereida ignava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Nereida.
OX   NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK74845.1, ECO:0000313|Proteomes:UP000048949};
RN   [1] {ECO:0000313|EMBL:CRK74845.1, ECO:0000313|Proteomes:UP000048949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK74845.1,
RC   ECO:0000313|Proteomes:UP000048949};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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; CVQV01000004; CRK74845.1; -; Genomic_DNA.
DR   RefSeq; WP_048598269.1; NZ_CVQV01000004.1.
DR   AlphaFoldDB; A0A0U1NJG9; -.
DR   STRING; 282199.GCA_001049735_00884; -.
DR   OrthoDB; 9812991at2; -.
DR   Proteomes; UP000048949; 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:CRK74845.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:CRK74845.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048949};
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"
SQ   SEQUENCE   294 AA;  32929 MW;  74DAD52B8C5AECBA CRC64;
     MRKNIYILPI LVIVVATALS SIFIVDERNK ALVLRFGQIV NVVEEPGLGF KVPLLDEVVR
     YEDRILSLQT PTIEVTPADD RRLEVDAFVL YRIADIIQFR QAVSFGGLRE AEAQLENILD
     GQIRAVLGSE GVTSNTILSP ERSALMENIR VQAAARADAL GLAVVEVRLR QTNLPEQNFD
     ATLQRMIAER DREATDERAR GREAASRVRA LADRTYDEII AEATRDARII EGEADAERNR
     IFAEAYTKDP EFFEFYRSLA AYEEAIKGSN STLVLSPDSE FFNYLRSDTG ASAN
//
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