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TAGH_ALKCK
ID   TAGH_ALKCK              Reviewed;         360 AA.
AC   Q5WCL2;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Teichoic acids export ATP-binding protein TagH {ECO:0000255|HAMAP-Rule:MF_01715};
DE            EC=7.5.2.4 {ECO:0000255|HAMAP-Rule:MF_01715};
GN   Name=tagH {ECO:0000255|HAMAP-Rule:MF_01715}; OrderedLocusNames=ABC3365;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the ABC transporter complex TagGH involved in
CC       teichoic acids export. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01715}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + teichoic acidSide 1 = ADP + phosphate + teichoic
CC         acidSide 2.; EC=7.5.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01715};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TagH) and
CC       two transmembrane proteins (TagG). {ECO:0000255|HAMAP-Rule:MF_01715}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01715};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01715}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Teichoic acids
CC       exporter (TC 3.A.1.104.1) family. {ECO:0000255|HAMAP-Rule:MF_01715}.
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DR   EMBL; AP006627; BAD65898.1; -; Genomic_DNA.
DR   RefSeq; WP_011248204.1; NC_006582.1.
DR   AlphaFoldDB; Q5WCL2; -.
DR   SMR; Q5WCL2; -.
DR   STRING; 66692.ABC3365; -.
DR   EnsemblBacteria; BAD65898; BAD65898; ABC3365.
DR   KEGG; bcl:ABC3365; -.
DR   eggNOG; COG1134; Bacteria.
DR   HOGENOM; CLU_000604_101_8_9; -.
DR   OMA; VHIVYRV; -.
DR   OrthoDB; 887953at2; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015438; F:ABC-type teichoic acid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03220; ABC_KpsT_Wzt; 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; IPR015860; ABC_transpr_TagH-like.
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.
DR   PROSITE; PS51251; TAGH; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..360
FT                   /note="Teichoic acids export ATP-binding protein TagH"
FT                   /id="PRO_0000092987"
FT   DOMAIN          24..245
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
FT   REGION          246..360
FT                   /note="Unknown"
FT   REGION          270..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         59..66
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
SQ   SEQUENCE   360 AA;  40257 MW;  2837F8CDB260D000 CRC64;
     MNPKMILTGV SKKYTLYRNN TEKLKAMFFP KTREQHRDFY ALKDINLEVY EGETIGVIGI
     NGSGKSTISN ILASVIPPTE GEMTVNGETS LIAINVGLNK NLNGYENIEQ KCLMHGFSKK
     EIEELMPAIE EFADIGDFID QPVKSYSSGM KSRLGFAISA HTNPDILIVD EALSVGDKTF
     YQKCKDKIDE FKAQNKTIVF ISHNIKEIKN LSDRVLWLHN GEVREFGDKN EVIKQYEDYI
     NWFNKLSKEE KEAHKQELKE MRSLAPSLYE EQENGKAGSG GDGTQPIVQP KRDKQAVKSA
     VWFFSQLVVF AVIFLTAAYF LVVPQLTDGS GSEELEQVAV GAEVQAGTSM GDIDNSDVSL
 
 
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