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Y1216_LISMF
ID   Y1216_LISMF             Reviewed;         268 AA.
AC   Q720M2;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative ABC transporter ATP-binding protein LMOf2365_1216;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=LMOf2365_1216;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC       energy coupling to the transport system (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE017262; AAT03992.1; -; Genomic_DNA.
DR   RefSeq; WP_003724739.1; NC_002973.6.
DR   AlphaFoldDB; Q720M2; -.
DR   SMR; Q720M2; -.
DR   KEGG; lmf:LMOf2365_1216; -.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; DIVPLYC; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR   GO; GO:0006824; P:cobalt ion transport; IEA:InterPro.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR005876; Co_trans_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01166; cbiO; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Translocase;
KW   Transport.
FT   CHAIN           1..268
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   LMOf2365_1216"
FT                   /id="PRO_0000092030"
FT   DOMAIN          2..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         35..42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   268 AA;  29835 MW;  2AF8B1A2508BE1A5 CRC64;
     MLKTEHISFQ YEDGKQALTD VSIDLEKGNI IGLIGANGSG KSTLFMQLLG INKPSDGTVY
     FEGKPLAYTK KALFALRKKV SIVFQDPDQQ IFYSNVRDDV AFALRNLGVS ETEVEARVTK
     VLDIVGAKDF QHKPVQYLSY GQKKRVAIAG ALVLDTDWLL LDEPTAGLDP IGKKIMMEII
     ERLASQGKKI LISSHDIDLI YEICDYVYML KDGSVLTDGE TSNVFLEKSN VEQAGLVQPW
     LIKLHQQAGY PLFKKEADFF AHTGKVTN
 
 
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