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Peptidoglycan glycosyltransferase (EC 2.4.1.129)

 C8W8H7_ATOPD            Unreviewed;       954 AA.
C8W8H7;
03-NOV-2009, integrated into UniProtKB/TrEMBL.
03-NOV-2009, sequence version 1.
25-OCT-2017, entry version 58.
SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ACV51768.1};
EC=2.4.1.129 {ECO:0000313|EMBL:ACV51768.1};
OrderedLocusNames=Apar_1344 {ECO:0000313|EMBL:ACV51768.1};
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI
0546) (Streptococcus parvulus) (Peptostreptococcus parvulus).
Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales;
Atopobiaceae; Atopobium.
NCBI_TaxID=521095 {ECO:0000313|EMBL:ACV51768.1, ECO:0000313|Proteomes:UP000000960};
[1] {ECO:0000313|EMBL:ACV51768.1, ECO:0000313|Proteomes:UP000000960}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546
{ECO:0000313|Proteomes:UP000000960};
PubMed=21304653; DOI=10.4056/sigs.29547;
Copeland A., Sikorski J., Lapidus A., Nolan M., Del Rio T.G.,
Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Pukall R.,
Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
Goodwin L., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
Palaniappan K., Chain P., Rohde M., Goker M., Bristow J., Eisen J.A.,
Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
"Complete genome sequence of Atopobium parvulum type strain (IPP
1246).";
Stand. Genomic Sci. 1:166-173(2009).
[2] {ECO:0000213|PDB:4JBF}
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 505-954.
Midwest Center For Structural Genomics (MCSG);
Filippova E.V., Wawrzak Z., Minasov G., Shuvalova L., Kiryukhina O.,
Babnigg G., Rubin E., Sacchettini J., Joachimiak A., Anderson W.F.;
"Crystal structure of peptidoglycan glycosyltransferase from Atopobium
parvulum DSM 20469.";
Submitted (FEB-2013) to the PDB data bank.
[3] {ECO:0000213|PDB:4N1X}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 515-954.
Filippova E.V., Minasov G., Shuvalova L., Kiryukhina O., Babnigg G.,
Rubin E., Sacchettini J., Joachimiak A., Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with penicillin G.";
Submitted (OCT-2013) to the PDB data bank.
[4] {ECO:0000213|PDB:4QJG}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 505-954.
Midwest Center For Structural Genomics (MCSG);
Filippova E.V., Minasov G., Kiryukhina O., Clancy S., Joachimiak A.,
Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with penicillin V.";
Submitted (JUN-2014) to the PDB data bank.
[5] {ECO:0000213|PDB:4R3J}
X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 505-954.
Filippova E.V., Minasov G., Kiryukhina O., Clancy S., Joachimiak A.,
Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with cefapirin.";
Submitted (AUG-2014) to the PDB data bank.
[6] {ECO:0000213|PDB:4R0Q}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 505-954.
Filippova E.V., Minasov G., Kiryukhina O., Clancy S., Joachimiak A.,
Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with cephalothin.";
Submitted (AUG-2014) to the PDB data bank.
[7] {ECO:0000213|PDB:4R1G}
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 505-954.
Filippova E.V., Minasov G., Kiryukhina O., Clancy S., Joachimiak A.,
Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with cloxacillin.";
Submitted (AUG-2014) to the PDB data bank.
[8] {ECO:0000213|PDB:4R23}
X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 505-954.
Filippova E.V., Minasov G., Kiryukhina O., Clancy S., Joachimiak A.,
Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with dicloxacillin.";
Submitted (AUG-2014) to the PDB data bank.
[9] {ECO:0000213|PDB:4RA7}
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 505-954.
Filippova E.V., Minasov G., Kiryukhina O., Clancy S., Joachimiak A.,
Anderson W.F.;
"Structure of a putative peptidoglycan glycosyltransferase from
Atopobium parvulum in complex with nafcillin.";
Submitted (SEP-2014) to the PDB data bank.
-!- SIMILARITY: Belongs to the SEDS family.
{ECO:0000256|SAAS:SAAS00587907}.
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EMBL; CP001721; ACV51768.1; -; Genomic_DNA.
RefSeq; WP_012809424.1; NC_013203.1.
PDB; 4JBF; X-ray; 1.92 A; A/B=505-954.
PDB; 4N1X; X-ray; 2.00 A; A/B=515-954.
PDB; 4QJG; X-ray; 1.85 A; A/B=505-954.
PDB; 4R0Q; X-ray; 2.00 A; A/B=505-954.
PDB; 4R1G; X-ray; 1.92 A; A/B=505-954.
PDB; 4R23; X-ray; 1.84 A; A/B=505-954.
PDB; 4R3J; X-ray; 2.44 A; A/B=505-954.
PDB; 4RA7; X-ray; 1.94 A; A/B=505-954.
PDBsum; 4JBF; -.
PDBsum; 4N1X; -.
PDBsum; 4QJG; -.
PDBsum; 4R0Q; -.
PDBsum; 4R1G; -.
PDBsum; 4R23; -.
PDBsum; 4R3J; -.
PDBsum; 4RA7; -.
SMR; C8W8H7; -.
STRING; 521095.Apar_1344; -.
EnsemblBacteria; ACV51768; ACV51768; Apar_1344.
KEGG; apv:Apar_1344; -.
eggNOG; ENOG4107QHZ; Bacteria.
eggNOG; COG0768; LUCA.
eggNOG; COG0772; LUCA.
HOGENOM; HOG000101245; -.
OMA; NAWFSAV; -.
OrthoDB; POG091H01X4; -.
Proteomes; UP000000960; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0051301; P:cell division; IEA:InterPro.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001182; FtsW/RodA.
InterPro; IPR036138; PBP_dimer_sf.
InterPro; IPR001460; PCN-bd_Tpept.
PANTHER; PTHR30474; PTHR30474; 1.
Pfam; PF01098; FTSW_RODA_SPOVE; 1.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF56519; SSF56519; 1.
SUPFAM; SSF56601; SSF56601; 2.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:4JBF, ECO:0000213|PDB:4N1X,
ECO:0000213|PDB:4QJG, ECO:0000213|PDB:4R0Q};
Complete proteome {ECO:0000313|Proteomes:UP000000960};
Glycosyltransferase {ECO:0000313|EMBL:ACV51768.1};
Membrane {ECO:0000256|SAAS:SAAS00481328, ECO:0000256|SAM:Phobius};
Reference proteome {ECO:0000313|Proteomes:UP000000960};
Transferase {ECO:0000313|EMBL:ACV51768.1};
Transmembrane {ECO:0000256|SAAS:SAAS00481328,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00481328,
ECO:0000256|SAM:Phobius}.
TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 44 63 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 70 87 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 93 114 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 126 144 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 164 180 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 200 219 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 225 241 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 246 265 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 330 351 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 363 384 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 396 415 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 484 505 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 631 941 Transpeptidase.
{ECO:0000259|Pfam:PF00905}.
SEQUENCE 954 AA; 100455 MW; 5E92680037B72EBE CRC64;
MEKAGGLRRN TELFLLFVGA IPVFLLYAMY MITARSTLSV ETMAVPIGLF AAFTVAHIAI
RFLAPAADPA ILPIVFVLSG IGITMVTRLS PNLAVNQTIW LFISVVVMIV VLAIIRNLDA
LADYKYSIGI LGVILLLLPI VIGQDRYGSR LWISFGPFTF QPGEIAKIAI TLFLAFYLAL
NREALSVSMR SVGPFRIPRF KMLLPLFVMW GISLIVVIFE RDLGSALLFF VFFVIMLYVA
TGRASYVFVS VALLAIGGVI LYHFFSHVQT RVNIWLDPFK DPSGDGFQIV QSLYSIADGG
LAGTGIDKGM PTLIPVVESD FIFSAIAEEM GLFGGAAIIT LFLLLTVRGL ATAARAKSDS
SAFAAAGLTS VLAFQTFLII AGVTKLMPLT GVTLPFMSQG GSSLLSSFII VALLLRAGDE
GTGRETELEP SKKVLDSQRL EISSGGAHAS SVLHGSHIRG GFDLQSEESG VLGRVALGKR
LTNLVTVFTL FFTVLLGNLT FLMVIDAPRL QALPTNNHTI AKSAYVQRGA IITSDGVTLA
ESVKQDDGTY VRNYPHDGMA SHTVGYISTQ YGTAGIESSM NETLTGHADH SDWRSALYSM
AGINTTGSSV VLTINSQMQA VAEAALQGYS GSIVVMDPST GAVLAKASSP SYTHAELGTI
IESGTGSQLV DRTTQALYSP GSSFKTVTLA AGIDTHKTTL DTTYSAPGTM EIGGGTIHNY
ANEDMGTIPL REAFARSSNT ALAQLGVALG ADNLVSYARA FGYGTALGQD FSTTPSLMPN
PAEMTTWELA WASCGLPVGE HASPAGPQTT VMQNAVIAAA IANGGVVMNP YIVDRVLSPE
GAVVSTTSPK SLGQAVSADT AAQVREAMLG VVESGTGMGA RVPGVKIAGK TGTADVENGN
FNSFFIGFAP YDHPTLVVSV VIEGNGENVL GYGAQVGGRV LAQCLNIQAL GAAS


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BM679 Peptidoglycan 0.1 ml
BM679 Peptidoglycan 0.1 ml


 

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