ID Q0AN22_MARMM Unreviewed; 292 AA.
AC Q0AN22;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN OrderedLocusNames=Mmar10_2023 {ECO:0000313|EMBL:ABI66315.1};
OS Maricaulis maris (strain MCS10).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI66315.1, ECO:0000313|Proteomes:UP000001964};
RN [1] {ECO:0000313|EMBL:ABI66315.1, ECO:0000313|Proteomes:UP000001964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI66315.1,
RC ECO:0000313|Proteomes:UP000001964};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000449; ABI66315.1; -; Genomic_DNA.
DR RefSeq; WP_011643960.1; NC_008347.1.
DR AlphaFoldDB; Q0AN22; -.
DR STRING; 394221.Mmar10_2023; -.
DR MEROPS; I87.001; -.
DR KEGG; mmr:Mmar10_2023; -.
DR eggNOG; COG0330; Bacteria.
DR HOGENOM; CLU_059167_3_0_5; -.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000001964; 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 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:ABI66315.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:ABI66315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001964};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 19..188
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 292 AA; 33136 MW; 5BF6F52EE66137E8 CRC64;
MIRTLGIIIL VVAVFIGLQS VYIVSETQQA LILRLGEPVD AVNETSEPDP GLHFKTPFIM
DVLIFDKRNL ELDLDAEEIL ASDQERLIVD AFLRYRITDP LRFYQTFRDE RGAVVRLEQI
MDDSLRGVIA SIPSSDVISG QRADLMTRVQ AAVEAQVLTG RFGIEVIDVR ILAADLPPQI
ADNVFERMRS ERQQEAAQYR AEGEQRATEI RADADRQASI IRAQARADAQ RLRGEGDARQ
NQIYAEAYNR DPEFFAFYRS MLAYEQAVQS GTPIVIPPDS EFFRYFRSET GE
//
