ID Q814P7_BACCR Unreviewed; 683 AA.
AC Q814P7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=BC_5375 {ECO:0000313|EMBL:AAP12237.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP12237.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP12237.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; AE016877; AAP12237.1; -; Genomic_DNA.
DR RefSeq; NP_835036.1; NC_004722.1.
DR RefSeq; WP_000372958.1; NZ_CP034551.1.
DR AlphaFoldDB; Q814P7; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; bce:BC5375; -.
DR PATRIC; fig|226900.8.peg.5551; -.
DR HOGENOM; CLU_006354_2_7_9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..234
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 325..601
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 683 AA; 76614 MW; 4A8944A7BE2FB49A CRC64;
MDQTMNPKLK KYKRLFFTAM FSCVLFFVFS FFVIIIVAKI MGPPPVAVPQ TSVFYANDDT
VIGQSNEIQK RYNVSLNEIS PYVKEATLSI EDQRFYKHHG FDVKRIAGAI VADLKAMAKV
QGASTITQQY ARNLYLDHDK TWKRKLLEAM YTIRLEVNYN KNHILEGYLN TIYYGHGAYG
IEAASRLYFD KTAKELTLAE ASMLAGIPKG PSVYSPFLKE DRAKGRQALI LDEMVKQGYI
TKQQATLAKK ETLTFASLDT KKVAEVAPYF QDAVQASLLR DVGLDEQALQ RGGLRIYTTL
DPKLQAVAEQ AVKDHIPDTT NIQTALVSMN PTTGEVAALV GGTDYNMSQF NRATQAVRQP
GSTFKPFLYY AALERGFTPA TRLKSEYTVF TLGDGVSKYK PKNYKDYYAD DFVTMAQALA
VSDNIYAVKT NLFLGDDTLA KTAKQFGIKS ALKDVPSLAL GTSPVKPIEM VNAYSMFANG
GKEVKPTFIR RIMDHEGNIL YDAHLESKQV LDKSKAFVME EMMTGMFNKK LSSYAAVTGQ
SMLSKLSRTY AGKSGSTETD SWMIGFTPQI VTGVWVGYDQ PKSISNVAEQ GYAKKIWTDT
MEKGLDGQPK KEFKQPSDVV AVNINPENGK IATKNCPISV KMYFAKGTEP TEYCMDHVDD
KEEFEKTTEE KKKTSWWKKY LPW
//
