ID A0A1Y2ZV04_9GAMM Unreviewed; 415 AA.
AC A0A1Y2ZV04;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN ORFNames=BCS42_07150 {ECO:0000313|EMBL:OTE95713.1};
OS Crenothrix sp. D3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=1880899 {ECO:0000313|EMBL:OTE95713.1, ECO:0000313|Proteomes:UP000198219};
RN [1] {ECO:0000313|EMBL:OTE95713.1, ECO:0000313|Proteomes:UP000198219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D3 {ECO:0000313|EMBL:OTE95713.1};
RA Oswald K., Graf J.S., Littman S., Tienken D., Brand A., Wehrli B.,
RA Albertsen M., Daims H., Wagner M., Kuypers M.M., Schubert C.J., Milucka J.;
RT "Crenothrix are major methane consumers in stratified lakes.";
RL ISME J. 0:0-0(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:OTE95713.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MBQZ01000062; OTE95713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2ZV04; -.
DR STRING; 1880899.BCS42_07150; -.
DR Proteomes; UP000198219; 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;
FT DOMAIN 78..258
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 45440 MW; BA32FC53BB985174 CRC64;
MSWNEPGGDN KDPWSGRGDD KKPPDLDEVI RSLQEKLAKI FGGGNGDDEN SSGGSSSNNS
LKGLGFVAGG VALLWGLSGF YIVDEGNNGV ETRFGKYTIT TQSGLNWHLP SPIERVDIIN
VKQQRFIEVG YRGVAGTEQT TNSNSVPKEA LMLTADENIV DVSLNVRYQV DNAKDFLFSI
ANPAATLKQV TESVERGVIG SSTMDYALTE GRSDIAMKIK TEIQEVMNRY HAGILVTEVN
LQDVQPPEEV QNSFVDAIKS REDKERLINE AQAYFNDVVP KARGAAARKK QESEGYKEQV
IAQATGEASR FSQLLAEYQK SPDVMRKRLY IEAMESVLSN TNTVMVDVKN GANNMLYLPL
DKLLQQQPPA TNGSNTAQTT TEPLPSIKPS VVEKSISVDR SAARGRDLRG RSDAE
//