ID A0A1H1HCC2_9GAMM Unreviewed; 376 AA.
AC A0A1H1HCC2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=SAMN05216569_3736 {ECO:0000313|EMBL:SDR23009.1};
OS Pseudoxanthomonas sp. CF125.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDR23009.1, ECO:0000313|Proteomes:UP000199049};
RN [1] {ECO:0000313|EMBL:SDR23009.1, ECO:0000313|Proteomes:UP000199049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF125 {ECO:0000313|EMBL:SDR23009.1,
RC ECO:0000313|Proteomes:UP000199049};
RA de Groot N.N.;
RL Submitted (OCT-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; FNLD01000004; SDR23009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1HCC2; -.
DR STRING; 1855303.SAMN05216569_3736; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000199049; 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:SDR23009.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:SDR23009.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199049}.
FT DOMAIN 70..230
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 376 AA; 40742 MW; E8105E3424CF0AA0 CRC64;
MAWNTPGSSS NGSNGDGEKP RPNPWKPKGN KGGGNDLNGL LDRLRGMFDG SGGNPLRWVV
IGLALLLVFS SFQLIGEQQR GVVLRFGQFA RIMQPGPNFK WPWPIESVTK VNATEIKTFS
NTVPVLTKDE NIVTVSLNVQ YRISDPRLYL FGSRNADEVL KQAAQSAVRE QVGRSDLDTV
LGVRGPLGSS AKERLQHSLD AYRTGLVVTE LNLPDARPPT EVQPAFDEVN SAQQVRESLV
NQAQAYAAKV VPEARGEAAR RRTTADGYKT AAVARATGDA ARFSLLQEQY KSAPEVTRKR
LWLETVQSVL AQNRKVVGGD GKQLIYVPMP AQNGAPAAPA PALLPNEAVM PAVQSTAPSS
SSERPARPTG REEVER
//
