ID I3CDS2_9GAMM Unreviewed; 292 AA.
AC I3CDS2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN ORFNames=BegalDRAFT_0857 {ECO:0000313|EMBL:EIJ41765.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41765.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ41765.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41765.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) 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; JH600070; EIJ41765.1; -; Genomic_DNA.
DR RefSeq; WP_002684008.1; NZ_JH600070.1.
DR AlphaFoldDB; I3CDS2; -.
DR STRING; 395493.BegalDRAFT_0857; -.
DR MEROPS; I87.001; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_059167_3_0_6; -.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000005744; 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:EIJ41765.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:EIJ41765.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005744};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..184
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 292 AA; 33304 MW; D077931AAE40B4E3 CRC64;
MLQNKMILGA ISIVVLLILM MSMFYVQETE KALKLQFGRV VKSDYTPGLH FKVPFLQTIR
KFDARIQSFD SNPQHFLTGE QKNLIVDSFI KWRITDTETY FKSVGGNPIN AGRRLSEFIA
DGLRSEFGKR TIQEVVSGDR AKIMDIITAE ANRRGNEFGI EVVDVRIKQI NLPDDVSTSV
YQRMDAAREQ VARELRSRGE AAATRIRAEA DRENMEIISK AERDAEQIRG EGDATATEIY
ANAFSRNPDF YSFTRSLTAY RETFKSKDDI LLLEPDSDFF KFFKGIETAP AH
//
