ID A0A1M6NNQ3_9CLOT Unreviewed; 319 AA.
AC A0A1M6NNQ3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=SAMN02745912_01793 {ECO:0000313|EMBL:SHJ97313.1};
OS Paramaledivibacter caminithermalis DSM 15212.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Paramaledivibacter.
OX NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHJ97313.1, ECO:0000313|Proteomes:UP000184465};
RN [1] {ECO:0000313|EMBL:SHJ97313.1, ECO:0000313|Proteomes:UP000184465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15212 {ECO:0000313|EMBL:SHJ97313.1,
RC ECO:0000313|Proteomes:UP000184465};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRAG01000018; SHJ97313.1; -; Genomic_DNA.
DR RefSeq; WP_073149072.1; NZ_FRAG01000018.1.
DR AlphaFoldDB; A0A1M6NNQ3; -.
DR STRING; 1121301.SAMN02745912_01793; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000184465; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 InterPro; IPR001972; Stomatin_HflK_fam.
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 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:SHJ97313.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:SHJ97313.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 24..205
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 319 AA; 36340 MW; 60781ED5A543706C CRC64;
METKILRFIL GIFFIIFAFI IVTSSFYTVE SGEQVIIERL GEKVKLVKDA GIKFKIPIID
RIIKVQTEAL RTIQYGYIAT EKPTTKKTAT YEDVAEEAII LTKGSYLINV EAMIQYKILD
AADYIYNVDD QLGTIRLAFE SVLRRNVQNK DLDDALLNKE RISSEVLPEL VKKTKSYGLG
IEIKSLKIQN ITVPSNVKAA YDDVNNAINE KTELLDKANR YKNEKLPGAR AKAYKLIQDA
EAYKAEKVSQ AKGDVENFVQ VYEKYKVAKD ITKTRLYLET MEKILTKVKN KYIIDSSNDN
VIKYLPINPK SITPVKEAQ
//
