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Database: UniProt
Entry: A0A2M8RYT6_9PAST
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ID   A0A2M8RYT6_9PAST        Unreviewed;       644 AA.
AC   A0A2M8RYT6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Macrolide ABC transporter permease/ATP-binding protein MacB {ECO:0000313|EMBL:PJG84063.1};
GN   ORFNames=CVP04_01015 {ECO:0000313|EMBL:PJG84063.1};
OS   Caviibacterium pharyngocola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Caviibacterium.
OX   NCBI_TaxID=28159 {ECO:0000313|EMBL:PJG84063.1, ECO:0000313|Proteomes:UP000230282};
RN   [1] {ECO:0000313|EMBL:PJG84063.1, ECO:0000313|Proteomes:UP000230282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7_3 {ECO:0000313|EMBL:PJG84063.1,
RC   ECO:0000313|Proteomes:UP000230282};
RA   Christensen H.;
RT   "Reclassification of Bisgaard taxon 5 as Caviibacterium pharyngocola gen.
RT   nov., sp. nov.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC       exporter (TC 3.A.1.122) family. {ECO:0000256|ARBA:ARBA00038388}.
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:PJG84063.1}.
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DR   EMBL; PHGZ01000003; PJG84063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8RYT6; -.
DR   OrthoDB; 9770036at2; -.
DR   Proteomes; UP000230282; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003838; ABC3_permease_dom.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR017911; MacB-like_ATP-bd.
DR   InterPro; IPR025857; MacB_PCD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR30572:SF14; MACROLIDE EXPORT ATP-BINDING_PERMEASE PROTEIN MACB; 1.
DR   PANTHER; PTHR30572; MEMBRANE COMPONENT OF TRANSPORTER-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF02687; FtsX; 1.
DR   Pfam; PF12704; MacB_PCD; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:PJG84063.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230282};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        519..544
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        564..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        603..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..242
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   644 AA;  70601 MW;  B4E264643B244E3D CRC64;
     MNIIEIKNIN KYFGEGENRT QVLKDINLEI KKGDFIAIIG QSGSGKSTLM NIIGCLDTAT
     SGSYKIEETE VSRLNADQLS DLRRKKFGFI FQRYNLLSTL SAVENVALPA IYAGVDQKTR
     LERAALLLEK LGLADRLQNK PNQLSGGQQQ RVSIARALMN GGDIILADEP TGALDSRSGE
     TVMEILQQLH REGHTIILVT HDKQVAEFAN RIIEIKDGKI IEDTRKSDLI AQKEETAAPQ
     KSRFGFYKDQ FAESFKMSVK AIIAHKLRSL LTMLGIIIGI TSVVCVVALG NGSQQKILAN
     INSMGTNTMD IYNGTGFGDR RADKMQNLTV GDSNILAKQS YIESATPNSS VSGTLVYQNE
     SFTAQVKGVG DQYFNVKGLS LKQGQFFNDN DVKHNEQVAV IDENTLKQVF NNQNPIGQVL
     MLNKKPLRVI GVAATSNNMG MNSSSLNIYI PYSTAMNKIS GNQKIDSITV KVRNEVNSTV
     AEKDLTNLLL VRHGKKDFFV MNTDTIKQTI ESTTNTMRLL ISCIALISLV VGGIGVMNIM
     LVSVTERTKE IGVRMAIGAR QFNILQQFLI EAVLICLIGG LTGITLSILF GMLFNFFMTD
     FTMVFSSASI ISAVLCSTLI GIVFGYMPAK NAAKLNPITA LARE
//
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