ID A0A244E1U7_9BURK Unreviewed; 443 AA.
AC A0A244E1U7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=A8M77_32695 {ECO:0000313|EMBL:OUL98225.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUL98225.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUL98225.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUL98225.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
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:OUL98225.1}.
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DR EMBL; LYMK01000076; OUL98225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244E1U7; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000195166; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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 SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Reference proteome {ECO:0000313|Proteomes:UP000195166};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 112..287
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 48027 MW; 102B9DBE5322E206 CRC64;
MFNLNDGRWG RGDEPSSNSD RPNANRPDED SGPSGNNNRP RGQGPNQGPP DLDELWRDFN
RKLGGLFGGG RGGNGGRPNG GNGGNGMKPD MKNAGVGLGL VAAVAVLIWL GTGFFIVNEG
QQAVITQFGR YKATVGAGFN WRLPYPIQRH EIVVVTQIRS MDVGRDTIVR STGLRDSAML
TEDENIVEIK FAVQYRLSDA RAYLYESKTP TDAVVQVAET AVREVVGKMK MDAALAEERD
QIAPRVRALM QNILDRYKVG IEVVGINLQQ GGLRPPEQVQ AAFDDVLKAG QERERTKNEA
QAYANDVVPR ATGTASRLKE ESEAYKARII AQAQGDAQRF SSVLAEYQRA PQVTRDRMYT
DAMQQIYTNT TKVLVDSKQG SNLLYLPLDK LVQMSGQGAA GAPADGASPS VAGTAPTQSS
VIPVAPPGES RARDGRSRDR DVR
//
