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Database: UniProt
Entry: A0A1Y2ZV04_9GAMM
LinkDB: A0A1Y2ZV04_9GAMM
Original site: A0A1Y2ZV04_9GAMM 
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}.
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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
//
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