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Database: UniProt
Entry: A0A0P6XC15_9SPHN
LinkDB: A0A0P6XC15_9SPHN
Original site: A0A0P6XC15_9SPHN 
ID   A0A0P6XC15_9SPHN        Unreviewed;       325 AA.
AC   A0A0P6XC15;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Protein QmcA {ECO:0000256|ARBA:ARBA00017055};
GN   ORFNames=SZ64_12275 {ECO:0000313|EMBL:KPL68801.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL68801.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL68801.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL68801.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC       {ECO:0000256|ARBA:ARBA00008164}.
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:KPL68801.1}.
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DR   EMBL; JXQC01000003; KPL68801.1; -; Genomic_DNA.
DR   RefSeq; WP_054531076.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6XC15; -.
DR   STRING; 1603897.SZ64_12275; -.
DR   PATRIC; fig|1603897.4.peg.2394; -.
DR   OrthoDB; 9809197at2; -.
DR   Proteomes; UP000049978; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   CDD; cd08829; SPFH_paraslipin; 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; IPR018080; Band_7/stomatin-like_CS.
DR   InterPro; IPR001972; Stomatin_HflK_fam.
DR   PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43327:SF10; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR   PROSITE; PS01270; BAND_7; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049978};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          18..176
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          299..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..318
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   325 AA;  35223 MW;  1FD5A5AC0271578E CRC64;
     MSGFLIAILV VVFMFLMMGV RVVRQGYVYT IERLGKFTLA AEPGLHLIIP FIDRVGQKVN
     MMEQVLDIPG QEIITRDNAM VGVDAVVFFQ VLDAGKAAYE VHNLYLSIMA LTTTNLRTVM
     GSMDLDETLS KRDEINAKLL SVVDHATAPW GVKITRVEIK DIRPPRDISD AMTRQMKAER
     EKRAEILEAE GKRASDILRA EGLKQSQILA AEGRRESAFR DAEAREREAE AEARATQMVS
     DAIASSGSKA INYFIAQKYT DAVGKFATSP NAKTILFPVE ATQLIGSLGG IGELVKDAVG
     GGSAPPAPTP PPAPRRSVPP AGGGQ
//
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