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Y339_CHLMU
ID   Y339_CHLMU              Reviewed;         259 AA.
AC   Q9PKX1;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable metal transport system ATP-binding protein TC_0339;
GN   OrderedLocusNames=TC_0339;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Part of an ATP-driven transport system
CC       TC_0338/TC_0339/TC_0341/TC_0342 for a metal. Probably responsible for
CC       energy coupling to the transport system.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE002160; AAF39202.1; -; Genomic_DNA.
DR   PIR; G81714; G81714.
DR   RefSeq; WP_010230210.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKX1; -.
DR   SMR; Q9PKX1; -.
DR   STRING; 243161.TC_0339; -.
DR   EnsemblBacteria; AAF39202; AAF39202; TC_0339.
DR   GeneID; 1246383; -.
DR   KEGG; cmu:TC_0339; -.
DR   eggNOG; COG1121; Bacteria.
DR   HOGENOM; CLU_000604_1_11_0; -.
DR   OMA; SVWDVVM; -.
DR   OrthoDB; 1721927at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Transport.
FT   CHAIN           1..259
FT                   /note="Probable metal transport system ATP-binding protein
FT                   TC_0339"
FT                   /id="PRO_0000093229"
FT   DOMAIN          9..241
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         41..48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   259 AA;  28895 MW;  8EB8DE5AA7185994 CRC64;
     MNRDNTIAWA VDDLCVNYDH SDVLCHIAFS LPSGAMAAII GPNGAGKSTL LKASLGLIRA
     SSGQSLFFGQ KFAKVHQRIA YMPQRASVDW DFPMTVLDLV LMGCYGYKGM WNRISTGDRR
     EAMNILERVG LADFANRQIG KLSGGQQQRA FLARSLMQKA DLYLMDELFS AIDMASYRMV
     VDVLQDLKKE GKTIVVIHHD LSNVRQLFDH VILLNKHLVC SGSVEKCLTK EAIFQAYGCE
     LELLDYTLKL SRGKYQGSC
 
 
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