ID A0A0M3TUL5_9GAMM Unreviewed; 285 AA.
AC A0A0M3TUL5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN ORFNames=SP60_08010 {ECO:0000313|EMBL:ALE53135.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE53135.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE53135.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE53135.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
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; CP010552; ALE53135.1; -; Genomic_DNA.
DR RefSeq; WP_053952131.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M3TUL5; -.
DR STRING; 1705394.SP60_08010; -.
DR KEGG; tho:SP60_08010; -.
DR PATRIC; fig|1705394.5.peg.1602; -.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000058020; Chromosome.
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:ALE53135.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:ALE53135.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000058020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 18..181
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 285 AA; 32408 MW; 9D42EE5586A467AD CRC64;
MKKLGLIIIA AVFFVLSSAL YTVNETQTAI KLRLGEIVSV EKEPGLKLKM PFVNNVVKFD
DRVQTLDAPS ERFLTGEKKN VIVDSYVKWR INDAEQFYKS TGGNLARTDN RLAQIIKTGL
KSEFSKRTIA DVVSGERGEI MSNIVKLAKK DISEFGIEIV DVRIKRIDLS QEVSNSVYRR
MQAERQRVAK EFRSKGAEEA EIIRAAADKE RTIILANAYR DSEMIRGEGD AISAGNYAQA
YNENVDFYSF YRSLESYKKS FSGQNDIMVL NPNTEFFRHF NPEVK
//
