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Database: UniProt
Entry: E3D4V7_NEIM7
LinkDB: E3D4V7_NEIM7
Original site: E3D4V7_NEIM7 
ID   E3D4V7_NEIM7            Unreviewed;       640 AA.
AC   E3D4V7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:ADO31639.1};
GN   OrderedLocusNames=NMBB_1311 {ECO:0000313|EMBL:ADO31639.1};
OS   Neisseria meningitidis serogroup B (strain alpha710).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO31639.1, ECO:0000313|Proteomes:UP000006929};
RN   [1] {ECO:0000313|EMBL:ADO31639.1, ECO:0000313|Proteomes:UP000006929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alpha710 {ECO:0000313|Proteomes:UP000006929};
RX   PubMed=20709895; DOI=10.1128/JB.00883-10;
RA   Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H.,
RA   Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.;
RT   "Comparative genome biology of a serogroup B carriage and disease strain
RT   supports a polygenic nature of meningococcal virulence.";
RL   J. Bacteriol. 192:5363-5377(2010).
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DR   EMBL; CP001561; ADO31639.1; -; Genomic_DNA.
DR   RefSeq; WP_014575373.1; NC_017505.1.
DR   AlphaFoldDB; E3D4V7; -.
DR   KEGG; nmp:NMBB_1311; -.
DR   PATRIC; fig|630588.3.peg.1510; -.
DR   HOGENOM; CLU_000604_36_0_4; -.
DR   OMA; CTHIADI; -.
DR   Proteomes; UP000006929; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
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   PANTHER; PTHR19211:SF14; ATP-BINDING CASSETTE SUB-FAMILY F MEMBER 1; 1.
DR   PANTHER; PTHR19211; ATP-BINDING TRANSPORT PROTEIN-RELATED; 1.
DR   Pfam; PF00005; ABC_tran; 2.
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, ECO:0000313|EMBL:ADO31639.1};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          2..246
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          313..527
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   COILED          84..111
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          591..618
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   640 AA;  71729 MW;  4930465E7C0B9D09 CRC64;
     MIEIKNLTLQ RGLKVLLDKA NATVNPGQRV GLIGKNGTGK SSLFALIKGE ITQDGGDVSI
     PKNWRLASVS QETPDLDISA LDYVLQGDAE LQTLQTALRQ AEAQNDGMKQ AEYHAKLEEI
     DAYTAPARAA KLLNGLGFSQ EEHSRPVKSF SGGWRMRLNL AQALICRADL LLLDEPTNHL
     DLETVLWLEN HLASLPCTQI IISHDRDFLN AATTQTIELS QQKLTQYGGN YDFYQNERAQ
     RLAQQQAAYV KQQAQIKHLQ SFIDRFKAKA TKAVQAQSRM KALAKLERIA PAHLDSEFSF
     EFYNPEHLPN PLLKLEHADL GYEGKTVLHD ITLSLESGAR YGLLGVNGSG KSTFIKALAG
     KIDLLSGSIV RSEKLNIGYF AQHQLDTIRA DQNPVWHIQQ LSPEVREQEI RNFLGGFNFV
     GDMALQKTEP FSGGEKARLA LAMIIWQKPN LLLLDEPTNH LDLDMRHALT LALQSFQGAL
     IAVSHDRSLL EATTDSFLLI DKGRLKNFDG DLNDYRQWRL AQENAAAAPA ASAQSQSRKD
     TKRIEAQIRQ EKARRGKPIQ QKIDRAEKEI ARLTDIQTAC EAFLAQEDAY LEANKEKLQN
     TLSQLAKVKT QLAQIEEVWL ACQEELERIE TEIEKQFAER
//
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