ID C0D5D3_9FIRM Unreviewed; 354 AA.
AC C0D5D3;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:EEG53445.1};
GN ORFNames=CLOSTASPAR_04479 {ECO:0000313|EMBL:EEG53445.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG53445.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG53445.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG53445.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG53445.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG53445.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: HflC and HflK could encode or regulate a protease.
CC {ECO:0000256|RuleBase:RU364113}.
CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex.
CC {ECO:0000256|RuleBase:RU364113}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364113}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily.
CC {ECO:0000256|ARBA:ARBA00006971, ECO:0000256|RuleBase:RU364113}.
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:EEG53445.1}.
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DR EMBL; ACCJ01000366; EEG53445.1; -; Genomic_DNA.
DR AlphaFoldDB; C0D5D3; -.
DR HOGENOM; CLU_039173_0_0_9; -.
DR Proteomes; UP000004756; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03404; SPFH_HflK; 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; IPR010201; HflK.
DR NCBIfam; TIGR01933; hflK; 1.
DR PANTHER; PTHR43327:SF2; MODULATOR OF FTSH PROTEASE HFLK; 1.
DR PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR Pfam; PF01145; Band_7; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 59..242
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 354 AA; 39242 MW; 14B63C1F6A21D091 CRC64;
MNIFGGNSFM NQYNKAKMNQ QAQPQGNPQG GGAGKGARSV LFAFKMVILI LFLGVTALQS
FYTLSENEMA VITTLGSPSS VTTSGFKFKW PYIQQVHKMS KEIRGMSIGY DPDYDPYNHA
NSENNPMTVP SEAEMITNDF NFVNVDFYIE YQIVDPVRAY INSESAISIL RNLAQSYIRD
TVGSYGVDEV ITTGKAEIQT KVKTLLTERL EQEDIGYGIN NVTIQDAVPP TDAVNDAFKA
VEDAKQGMDT KLNEAKKYQS EQLPAANAKA DKALKDAEAF KQERISEAEG QVSRFNDMYD
EYAKYPLITK KRMFYEMMEE VLPGLKVIVD GSDGTQTVLP LDSFVDGNAK GGAE
//