GenomeNet

Database: UniProt
Entry: A0A2N0EQM9_9FLAO
LinkDB: A0A2N0EQM9_9FLAO
Original site: A0A2N0EQM9_9FLAO 
ID   A0A2N0EQM9_9FLAO        Unreviewed;       235 AA.
AC   A0A2N0EQM9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Modulator of FtsH protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATE92_0474 {ECO:0000313|EMBL:PKA82346.1};
OS   Ulvibacter sp. MAR_2010_11.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacter.
OX   NCBI_TaxID=1250229 {ECO:0000313|EMBL:PKA82346.1, ECO:0000313|Proteomes:UP000232889};
RN   [1] {ECO:0000313|EMBL:PKA82346.1, ECO:0000313|Proteomes:UP000232889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_11 {ECO:0000313|EMBL:PKA82346.1,
RC   ECO:0000313|Proteomes:UP000232889};
RA   Teeling H.;
RT   "A large-scale integrated study on North Sea by COGITO (Coastal Microbe
RT   Genomic & Taxonomic Observatory).";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the BI1 family. {ECO:0000256|ARBA:ARBA00010350,
CC       ECO:0000256|RuleBase:RU004379}.
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:PKA82346.1}.
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; PHTY01000001; PKA82346.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0EQM9; -.
DR   OrthoDB; 5177430at2; -.
DR   Proteomes; UP000232889; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006214; Bax_inhibitor_1-related.
DR   PANTHER; PTHR23291:SF32; BAX INHIBITOR 1; 1.
DR   PANTHER; PTHR23291; BAX INHIBITOR-RELATED; 1.
DR   Pfam; PF01027; Bax1-I; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU004379};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU004379};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU004379}.
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        95..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        124..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        157..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        180..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU004379"
SQ   SEQUENCE   235 AA;  26174 MW;  E2BBEFA0F02D548F CRC64;
     MEQIQPQQHI SVAGLTDEKR VAFYRKTYTH LALAVLLFIL VEMIFFQIPA LLQFALSLTQ
     GWLWLVMLGG FMLVTNYAEK MALNSHDINK QYLALLLFVI AEAFIFIPLI FIAMSIAADG
     GMEILNQAAI MTLSLFSGLS AIVLLTKKDF SFLKSMLAIG FFIALGLIVA GVLFGFNLGL
     WFSVGMIILA SGAILYQTSN MVHKYSEDQY VAASLGLFAS LMLLFWYILS ILSRD
//
DBGET integrated database retrieval system