ID A0A4R3Y7A7_9PROT Unreviewed; 292 AA.
AC A0A4R3Y7A7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN ORFNames=EDC63_10560 {ECO:0000313|EMBL:TCV87391.1};
OS Sulfurirhabdus autotrophica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sulfuricellaceae; Sulfurirhabdus.
OX NCBI_TaxID=1706046 {ECO:0000313|EMBL:TCV87391.1, ECO:0000313|Proteomes:UP000295367};
RN [1] {ECO:0000313|EMBL:TCV87391.1, ECO:0000313|Proteomes:UP000295367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100309 {ECO:0000313|EMBL:TCV87391.1,
RC ECO:0000313|Proteomes:UP000295367};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TCV87391.1}.
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DR EMBL; SMCO01000005; TCV87391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R3Y7A7; -.
DR Proteomes; UP000295367; 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 InterPro; IPR001972; Stomatin_HflK_fam.
DR NCBIfam; TIGR01932; hflC; 1.
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 PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:TCV87391.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:TCV87391.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295367};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 21..185
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 292 AA; 33281 MW; 325B7C614EC520C0 CRC64;
MMKNLGTILI GIILVLVVLS LAMFTVDQRQ NAIIFQLGEV VAVKKQPGLY FKIPLIQNVR
YFDTRILTID TGEPERFITS EKKNVLVDSF VKWRIVDVKQ YYVSVGGDEM RAQTRLMQTV
NDGLRAEFGK RTVHDVVSGE RDQIMEILRT KANQDASKIG VQVIDVRLKR VDLPQEVSDS
VYRRMEAERK RVANELRSTG AAEAEKIRAD ADKQREVIIA EAYRDAQRIK GEGDAKASGI
YAAAYSQSPE FYAFYRSMEA YRQSFKNKSD VMILEPTSEF FKYLKNPGKT GK
//
