ID   TAGH_LACLA              Reviewed;         466 AA.
AC   Q9CH26;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=LL0915;
GN   ORFNames=L137446;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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; AE005176; AAK05013.1; -; Genomic_DNA.
DR   PIR; C86739; C86739.
DR   RefSeq; NP_267071.1; NC_002662.1.
DR   RefSeq; WP_003131432.1; NC_002662.1.
DR   AlphaFoldDB; Q9CH26; -.
DR   SMR; Q9CH26; -.
DR   STRING; 272623.L137446; -.
DR   PaxDb; Q9CH26; -.
DR   EnsemblBacteria; AAK05013; AAK05013; L137446.
DR   KEGG; lla:L137446; -.
DR   PATRIC; fig|272623.7.peg.980; -.
DR   eggNOG; COG1134; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_000604_101_8_9; -.
DR   OMA; RRDEPRM; -.
DR   Proteomes; UP000002196; 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   CDD; cd00118; LysM; 1.
DR   Gene3D; 3.10.350.10; -; 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; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51782; LYSM; 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..466
FT                   /note="Teichoic acids export ATP-binding protein TagH"
FT                   /id="PRO_0000092990"
FT   DOMAIN          27..249
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
FT   DOMAIN          403..447
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   REGION          250..466
FT                   /note="Unknown"
FT   REGION          356..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..466
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01715"
SQ   SEQUENCE   466 AA;  52210 MW;  3A35DCD621656C48 CRC64;
     MNTNKVKIKA EYLTKKFELL PAKSSKNKAK SLIGSNSKNE KDFWALRNIS FEIRDGECVG
     VIGLNGAGKS TLSNIISGQI AQTTGRVEIN GDVSIIAASA GMQNNLSGRE NIRLKALMVG
     LTNKEIKSKM DDIIEFSELG PFIDQPVKTY SSGMKAKLGF SIMVHQNPDI MIIDEGLSVG
     DKTFVDKSQK KMFEFRDEGK TILLVSHDMR TIKEWCDRVI WLNYGEVKAY GRPEEVIPEY
     EKFVQWFKKL PKKEQEKFKT DQRQAQLDYS VEELKAEIVS QNPSKSRRVQ REVTEELKNK
     KDNHKLSLMS KVIVWLCLLA FIWITLVSLS NATLAESLRH PKTFFTERLF KSDTRNMTST
     TKKEAVVKTS SSPKKKVSQA KKTTKVSSTQ KNTSSSSSTS NQNTYIVQAG DSLSIIAENH
     GYSVEEIQQV NPGVDFSVIH PGQEINLPEP TTSANSTTEQ SDGANQ