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Database: UniProt
Entry: A0A562J282_9GAMM
LinkDB: A0A562J282_9GAMM
Original site: A0A562J282_9GAMM 
ID   A0A562J282_9GAMM        Unreviewed;       394 AA.
AC   A0A562J282;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN   ORFNames=LX59_00128 {ECO:0000313|EMBL:TWH77223.1};
OS   Azomonas agilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azomonas.
OX   NCBI_TaxID=116849 {ECO:0000313|EMBL:TWH77223.1, ECO:0000313|Proteomes:UP000319627};
RN   [1] {ECO:0000313|EMBL:TWH77223.1, ECO:0000313|Proteomes:UP000319627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 375 {ECO:0000313|EMBL:TWH77223.1,
RC   ECO:0000313|Proteomes:UP000319627};
RA   Kyrpides N.;
RT   "Genomic Encyclopedia of Type Strains, Phase I: the one thousand microbial
RT   genomes (KMG-I) project.";
RL   Submitted (JUL-2019) 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:TWH77223.1}.
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DR   EMBL; VLKG01000001; TWH77223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A562J282; -.
DR   OrthoDB; 9779595at2; -.
DR   Proteomes; UP000319627; 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; IPR020980; Membrane_HflK_N.
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   Pfam; PF12221; HflK_N; 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:TWH77223.1};
KW   Membrane {ECO:0000256|RuleBase:RU364113};
KW   Protease {ECO:0000313|EMBL:TWH77223.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000319627};
KW   Transmembrane {ECO:0000256|RuleBase:RU364113};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU364113"
FT   DOMAIN          87..247
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..394
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"
FT   COMPBIAS        20..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..380
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   394 AA;  43696 MW;  62A64A8EE0817B2C CRC64;
     MAWNEPGGNS NNQDQDPWGK GGRRGGDHQG PPDLDEAFRK LQDSLNSLFG GKKRGSDSGD
     NNSGASGGGF GMLWLGLVVL FGFWLYNAVY IVDEQEQAVI LRFGKYYETV GPGLNLYFPP
     IDTKFQENVT RERSYSKQGQ MLTQDENIIE VPLTVQYKVG NLKDFVLAVD EPEISLQQAT
     DSAVRHVVGS TAMDQVLTEG REAMAGEVKE RLQRFMERYN TGIVVTQVNL QSAAAPREVQ
     EAFDDVIRAR EDEQRLKNQA ESYANGVVPE ARGEAQRMLE EASGYRESVI ARAEGEANRF
     SKLREEYSKA PEVTRERLYL ETMQQIMGNT SKVLITAEQG QNSLLYLPLD KMINSSKSSS
     YSGSSGNSNT SAQQEAVPVT NLPEQPDPRS RGGR
//
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