ID   TAGH_LISMF              Reviewed;         335 AA.
AC   Q720Z5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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};
GN   OrderedLocusNames=LMOf2365_1092;
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: 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; AE017262; AAT03869.1; -; Genomic_DNA.
DR   RefSeq; WP_003726883.1; NC_002973.6.
DR   AlphaFoldDB; Q720Z5; -.
DR   SMR; Q720Z5; -.
DR   KEGG; lmf:LMOf2365_1092; -.
DR   HOGENOM; CLU_000604_1_2_9; -.
DR   OMA; AVDAEFM; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015438; F:ABC-type teichoic acid transporter activity; ISS:JCVI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:JCVI.
DR   GO; GO:0015777; P:teichoic acid transport; ISS:JCVI.
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; Translocase;
KW   Transport.
FT   CHAIN           1..335
FT                   /note="Teichoic acids export ATP-binding protein TagH"
FT                   /id="PRO_0000092993"
FT   DOMAIN          26..246
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
FT   BINDING         60..67
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
SQ   SEQUENCE   335 AA;  37786 MW;  D36DB6CFA0F04BF9 CRC64;
     MGKNIKVSFK HVSKEYDLYQ NKSDKIKGLF MPKSQKMQSF WALRDVSFDI HDGETVGLIG
     INGSGKSTIS SIMSGVIPPT QGEVIINGET SLIAIAVGLK GPLTGYENIR LKLLMHGMKS
     SQINKLMPSI IEFADIGDFI NQPIKNYSSG MRSRLGFAIS VHTNPDILVI DEALSVGDQT
     FYEKCVDKIN EFKARGKTIV FVSHSLGQVK SLCDRIIWMH HGEIREMGTA QEVAQKYDEF
     VKWFNKQPND YKKKYQKEHK ENQKAPQKKI YPNPNANKYR LTLFDKIFLT VLIALTILFG
     TLVATGKSFK GLISEESTTQ IEKVVHVDNY DLKLN