(data stored in SCRATCH zone)

SWISSPROT: Q8XD16_ECO57

ID   Q8XD16_ECO57            Unreviewed;       720 AA.
AC   Q8XD16; A0A0H3JCF0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 113.
DE   SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:BAB33966.2};
GN   Name=lapB {ECO:0000313|EMBL:BAB33966.2};
GN   ORFNames=ECs_0543 {ECO:0000313|EMBL:BAB33966.2};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB33966.2, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB33966.2, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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DR   EMBL; BA000007; BAB33966.2; -; Genomic_DNA.
DR   RefSeq; NP_308570.1; NC_002695.1.
DR   RefSeq; WP_000739054.1; NZ_SDVX01000001.1.
DR   PRIDE; Q8XD16; -.
DR   EnsemblBacteria; AAG54839; AAG54839; Z0634.
DR   GeneID; 915052; -.
DR   KEGG; ecs:ECs0543; -.
DR   PATRIC; fig|386585.9.peg.650; -.
DR   KO; K12541; -.
DR   BioCyc; ECOO157:Z0634-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017750; ATPase_T1SS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_I_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   TIGRFAMs; TIGR03375; type_I_sec_LssB; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   4: Predicted;
DR   PRODOM; Q8XD16.
DR   SWISS-2DPAGE; Q8XD16.
KW   ATP-binding {ECO:0000313|EMBL:BAB33966.2};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Nucleotide-binding {ECO:0000313|EMBL:BAB33966.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
SQ   SEQUENCE   720 AA;  80628 MW;  2AFE82605037A9EC CRC64;
     MKKNAQSVEA WLEAMIAVAR YYRLDFSQEN VRATVNWERD SKREELLTDM ARQLGMGLRL
     VEFSADSLNP WRLPLIAVFD NQQIGVITRR DNHDNISVQF SGDEGLETTL NVADIEDKIV
     ELALLRPLSA IPDARVDDYI RPYQANWFWS LSLKDWRRYG DIMLASLVAN VLALAAMIFS
     MQVYDRVVPA QSYPTLWVLF AGVMMAILFE FCMRMVRTHL SDVIGKRADL RISDRVFGHA
     LRLKNNVRSK STGSFISQIR ELESVRELIT STTIGAVADL PFFLLFVFIL WMIGGWLVLV
     VLLALPLLVI PGLLVQRPLA RLANEGMRES AVRNATLVEA VQSIEDIKLL RAEQRFQNQW
     NHTNDVASSI SMKQRFLTGL LLTWTQEVQS IVYVVVLLVG CFMVMNGDMT TGALVGTTIL
     ASRTIAPLSQ ISGVLSRWQQ AKVARNGLDE LMKRPVDQPE HGKLVHKAVL HGNYQFSNAV
     FYYDEEEKIA DVAIGKLNIQ AGEKIAILGR NGAGKSTLLQ MLAGMRIAQQ GQVLLDNISI
     GQLDPADLRR DMGLLSQTGR LFFGSLRENL TMGMPEASDE DIERALTLSG ALPFVQKQKN
     GLNYMIQEGG FGLSGGQRQT LLLARLLISQ PNIVLLDEPS ASLDEMAEAY LIEQLKQWIG
     HRTLIIATHR TAMLQLVDRI IVMDQGRIVM DGAKEAILRE QGEPTARRVV LQEKNKGSAA
//

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