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
//