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Database: UniProt
Entry: A0A149Q3X3_9PROT
LinkDB: A0A149Q3X3_9PROT
Original site: A0A149Q3X3_9PROT 
ID   A0A149Q3X3_9PROT        Unreviewed;       630 AA.
AC   A0A149Q3X3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Glycosyl transferase family 1 {ECO:0000313|EMBL:KXU92031.1};
GN   ORFNames=AD928_12635 {ECO:0000313|EMBL:KXU92031.1};
OS   Acetobacter cerevisiae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU92031.1, ECO:0000313|Proteomes:UP000075473};
RN   [1] {ECO:0000313|EMBL:KXU92031.1, ECO:0000313|Proteomes:UP000075473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU92031.1,
RC   ECO:0000313|Proteomes:UP000075473};
RA   Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT   "Improved classification and identification of acetic acid bacteria using
RT   matrix-assisted laser desorption/ionization time-of-flight mass
RT   spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT   heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT   respectively.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KXU92031.1}.
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DR   EMBL; LHZA01000156; KXU92031.1; -; Genomic_DNA.
DR   RefSeq; WP_062250934.1; NZ_LHZA01000156.1.
DR   AlphaFoldDB; A0A149Q3X3; -.
DR   PATRIC; fig|178900.5.peg.1866; -.
DR   Proteomes; UP000075473; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR032524; ABC_tran_C.
DR   InterPro; IPR032781; ABC_tran_Xtn.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 3; 1.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF16326; ABC_tran_CTD; 1.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075473};
KW   Transferase {ECO:0000313|EMBL:KXU92031.1}.
FT   DOMAIN          4..245
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          311..526
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          525..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          560..629
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        533..553
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  68774 MW;  F9DD7E5406785B45 CRC64;
     MSLLVISDLT LRIAGRTLLD HADLSIEPGR KVGLVGRNGA GKSTLLGAIA GDLAPDGGEI
     RLSSRARMAR VKQEAPADGA SLLDTVLAGD TERTALLTEA DTATDPVRIA EIHERLRAIQ
     ADSAPARAGS VLAGLGFSAE AQRRPVSDFS GGWRMRVSLA TALFLEPDLL LLDEPTNHLD
     LEATLWLEGW LTRFSGAALI VSHDRGLLDS CVDAIAHLDK GKLSLTPGGY ENFVRIRTEQ
     ALQQARAAER IAAQRAHMQS FVDRFRAKAT KARQAQARVK ALEKLPVIES VVEDTPTRFA
     FPEPEQLAPP MFTANRVTIG YGTTPILSNL SFRLDMEDRI ALLGANGNGK STLAKLIAGR
     LEPMSGSVER NSRLKIGYFA QHQAEELVLH QTPIDHMERA LPKALPPVVR AQLARFGLDA
     DRAETPVKDL SGGEKARLLL ALATRDAPQL LILDEPTNHL DLDARDALVR ALSEFEGAVL
     LISHDPHLVE MVADRLWLVA DGKVTPFDGD MADYRRWLIE QNRASNRSSK QDTSAHASRK
     DDRRERAEAR KAQAPLRKII RDAEAKLAKL ATERTKIETT LADPALYADG KADEVTRLNT
     RLAAIGKEQA DLEERWLEAE AEIESAAAED
//
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