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Database: UniProt
Entry: A0A0A3ZB37_9GAMM
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ID   A0A0A3ZB37_9GAMM        Unreviewed;       714 AA.
AC   A0A0A3ZB37;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=ABC transporter {ECO:0000313|EMBL:KGT94984.1};
GN   ORFNames=NG99_04885 {ECO:0000313|EMBL:KGT94984.1};
OS   Erwinia typographi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=371042 {ECO:0000313|EMBL:KGT94984.1, ECO:0000313|Proteomes:UP000030351};
RN   [1] {ECO:0000313|EMBL:KGT94984.1, ECO:0000313|Proteomes:UP000030351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M043b {ECO:0000313|EMBL:KGT94984.1,
RC   ECO:0000313|Proteomes:UP000030351};
RA   Chan K.-G., Tan W.-S.;
RT   "Genome sequence of Erwinia typographi M043b.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00034018};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug exporter-2
CC       (TC 3.A.1.117) family. {ECO:0000256|ARBA:ARBA00006526}.
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:KGT94984.1}.
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DR   EMBL; JRUQ01000019; KGT94984.1; -; Genomic_DNA.
DR   RefSeq; WP_034888993.1; NZ_JRUQ01000019.1.
DR   AlphaFoldDB; A0A0A3ZB37; -.
DR   STRING; 371042.NG99_04885; -.
DR   eggNOG; COG2274; Bacteria.
DR   OrthoDB; 6828292at2; -.
DR   Proteomes; UP000030351; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd18567; ABC_6TM_CvaB_RaxB_like; 1.
DR   CDD; cd02419; Peptidase_C39C; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR033838; CvaB_peptidase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF606; COLICIN V SECRETION-PROCESSING ATP-BINDING PROTEIN; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        159..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          20..139
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          173..452
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          490..712
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   714 AA;  79244 MW;  5A7A71D834A3AB52 CRC64;
     MSFINSLTFG WGRRLPMMQQ TQAAECGLAC VGMVANYYGH SIDLISLRRR FSTSLKGATL
     ADVMQMAHRL GMGGRALRLE VEELEKLRRP CILHWDLNHF VVLKKVHRNK ITIHDPARGI
     RDIPMDEVSR CFTGVALELV PSASFKPVEE KQSISMMSLV GSVIGIRSVF VQILILSVAM
     ELFGILSPFY MQWVMDQVLV SADYDLLSLL GIGFIIVVIL QNAISTLRAW VTTWFSSLLG
     VQWTTNVFTK LLGLPMSYFE ERHVGDIVSR FGSISTIQST LTSRFISTLL DGVMAFATLS
     MLFIYNSALT WLVIGLFVTY ALIRLVSYRP FRQANEDQIV TAARAQSQLL ETIRGAQAVK
     LNNKQETRMV AYANALVETT NKGIVIQRLS IGFSTLQGVI SGVGRVVLIW LAAKQVLDGN
     FSVGMLVAFI SFSDQFIGRA SGLIDALIEF RMLRLYGERL ADIVLTDAEE DMEASVAEPA
     RTASGAGPAM TVKGLKFRYS ETEPWVLDNC SFILKPGESV AIVGPSGQGK TTLAKLLLGL
     LKPQEGTIEV DGIDIRQQGM RSHRERIGCV MQDDILFAGS IADNISFFDS KCDQQRIEQA
     ARLAQIHDDI MVMPMGYQSL VGDMGSSLSG GQNQRVLLAR ALYRQPDILV LDEASSHLDV
     ERERLINQAI QLMPITRVII AHRPETIRSA DRIICLANGK AFELDYDTLI NVRQ
//
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