DLTB_BACSU
ID DLTB_BACSU Reviewed; 395 AA.
AC P39580;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Teichoic acid D-alanyltransferase {ECO:0000250|UniProtKB:Q5M4V4};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q5M4V4};
GN Name=dltB {ECO:0000303|PubMed:10694878}; OrderedLocusNames=BSU38510;
GN ORFNames=ipa-4r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION.
RX PubMed=7797557; DOI=10.1074/jbc.270.26.15598;
RA Perego M., Glaser P., Minutello A., Strauch M.A., Leopold K., Fischer W.;
RT "Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid
RT in Bacillus subtilis. Identification of genes and regulation.";
RL J. Biol. Chem. 270:15598-15606(1995).
RN [4]
RP GENE FAMILY, AND PROBABLE ACTIVE SITE.
RX PubMed=10694878; DOI=10.1016/s0968-0004(99)01539-x;
RA Hofmann K.;
RT "A superfamily of membrane-bound O-acyltransferases with implications for
RT wnt signaling.";
RL Trends Biochem. Sci. 25:111-112(2000).
RN [5]
RP FUNCTION, MUTAGENESIS OF HIS-281; SER-285; 297-VAL-PHE-298 AND HIS-328, AND
RP ACTIVE SITE.
RX PubMed=30283133; DOI=10.1038/s41586-018-0568-2;
RA Ma D., Wang Z., Merrikh C.N., Lang K.S., Lu P., Li X., Merrikh H., Rao Z.,
RA Xu W.;
RT "Crystal structure of a membrane-bound O-acyltransferase.";
RL Nature 562:286-290(2018).
CC -!- FUNCTION: O-acyltransferase that catalyzes D-alanylation of both
CC teichoic acid and lipoteichoic acid (LTA) (PubMed:30283133). D-
CC alanylation of LTA plays an important role in modulating the properties
CC of the cell wall in Gram-positive bacteria, influencing the net charge
CC of the cell wall (PubMed:7797557). Catalyzes D-alanylation from DltC
CC carrier protein (PubMed:30283133). {ECO:0000269|PubMed:30283133,
CC ECO:0000269|PubMed:7797557}.
CC -!- PATHWAY: Cell wall biogenesis; lipoteichoic acid biosynthesis.
CC {ECO:0000305|PubMed:7797557}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5M4V4};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5M4V4}.
CC -!- DOMAIN: Consists of a ring of transmembrane domains, which shield a
CC highly conserved extracellular structural funnel extending into the
CC middle of the lipid bilayer. The conserved catalytic His residue is
CC located at the bottom of this funnel and is connected to the
CC intracellular DltC through a narrow tunnel.
CC {ECO:0000250|UniProtKB:Q5M4V4}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51560.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15877.1; -; Genomic_DNA.
DR PIR; S39659; S39659.
DR RefSeq; NP_391730.1; NC_000964.3.
DR RefSeq; WP_003227327.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39580; -.
DR SMR; P39580; -.
DR STRING; 224308.BSU38510; -.
DR TCDB; 2.A.50.2.1; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR PaxDb; P39580; -.
DR PRIDE; P39580; -.
DR EnsemblBacteria; CAB15877; CAB15877; BSU_38510.
DR GeneID; 937360; -.
DR KEGG; bsu:BSU38510; -.
DR PATRIC; fig|224308.179.peg.4170; -.
DR eggNOG; COG1696; Bacteria.
DR InParanoid; P39580; -.
DR OMA; CYSMYLF; -.
DR PhylomeDB; P39580; -.
DR BioCyc; BSUB:BSU38510-MON; -.
DR BioCyc; MetaCyc:BSU38510-MON; -.
DR UniPathway; UPA00556; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0070395; P:lipoteichoic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR024194; Ac/AlaTfrase_AlgI/DltB.
DR InterPro; IPR024024; DltB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
DR PIRSF; PIRSF016636; AlgI_DltB; 1.
DR PIRSF; PIRSF500216; DltB; 1.
DR TIGRFAMs; TIGR04091; LTA_dltB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..395
FT /note="Teichoic acid D-alanyltransferase"
FT /id="PRO_0000213128"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 27..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..46
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 47..50
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..76
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 77..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 80..104
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 105..120
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 121..137
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 138..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 146..175
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 176..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 180..223
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 224
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..256
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 257..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 267..303
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 304..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 309..328
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 329..333
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 334..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q5M4V4"
FT TOPO_DOM 388..395
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT ACT_SITE 328
FT /evidence="ECO:0000269|PubMed:30283133,
FT ECO:0000305|PubMed:10694878"
FT MUTAGEN 281
FT /note="H->A: Does not affect D-alanylation of lipoteichoic
FT acid (LTA)."
FT /evidence="ECO:0000269|PubMed:30283133"
FT MUTAGEN 285
FT /note="S->A: Does not affect D-alanylation of lipoteichoic
FT acid (LTA)."
FT /evidence="ECO:0000269|PubMed:30283133"
FT MUTAGEN 297..298
FT /note="VF->DD: Abolished D-alanylation of lipoteichoic acid
FT (LTA)."
FT /evidence="ECO:0000269|PubMed:30283133"
FT MUTAGEN 328
FT /note="H->A: Abolished D-alanylation of lipoteichoic acid
FT (LTA)."
FT /evidence="ECO:0000269|PubMed:30283133"
SQ SEQUENCE 395 AA; 46736 MW; 7A22C7B711FD6571 CRC64;
MTPYSSFLFF ILLGILLLPT IILGLNGKRF QAYNMFISII ILALIFSHDL HGVIALCLFT
IWQVLLISGY LAYRQKANSG FVFCGAVIAS ILPLFLSKIW PFLSHPQPHH PPHNLISFLG
ISYLTFKGVQ LIMEARDGLL KEQLPLHRLL YFILFFPTIS SGPIDRYRRF VKDEQKAWTK
EEYADLLYTG IHKIFIGFLY KFIIGYAINT YFIMNLPAIT HNKILGNLLY MYGYSMYLFF
DFAGYTMFAV GVSYIMGIKS PENFNKPFIS KNIKDFWNRW HMSLSFWFRD YVFMRFVFWM
TKKKWIKNRM AVSNIGYFLL FMLMGVWHGL APQYIIYGLY HAVLMTCYNF FEKWNKKYKW
LPSNRWTTIL AIVITFHFVC FGFYIFSGKP FHHHH
