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Database: UniProt
Entry: G7Z8A7_AZOL4
LinkDB: G7Z8A7_AZOL4
Original site: G7Z8A7_AZOL4 
ID   G7Z8A7_AZOL4            Unreviewed;      1014 AA.
AC   G7Z8A7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   OrderedLocusNames=AZOLI_1958 {ECO:0000313|EMBL:CBS87206.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS87206.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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; FQ311868; CBS87206.1; -; Genomic_DNA.
DR   RefSeq; WP_014248208.1; NC_016622.1.
DR   AlphaFoldDB; G7Z8A7; -.
DR   STRING; 862719.AZOLI_1958; -.
DR   KEGG; ali:AZOLI_1958; -.
DR   HOGENOM; CLU_012369_0_0_5; -.
DR   OrthoDB; 7311221at2; -.
DR   Proteomes; UP000005667; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00912; Transgly; 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:ARBA00022670};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          142..334
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
SQ   SEQUENCE   1014 AA;  111980 MW;  C0CA77A01DE922BB CRC64;
     MAKAWVQAGR WARRAVIGVA LTTTVAAVGY AGWREMETSR LQARLLSGVA QSMTVSLREG
     PNPAARYPAH GPYNERLGYT ALPGQLDLLT RDIYAVEQQA VLSPALDRFM AGGGFPIYRE
     KTQAGLTLLD RNGVPMYAAR YPERVFDGFD DVPKLVADTL LFIENRELLN EDEPRRNPAV
     EWDRFGAAVA MLPLQMVRPG QRSPGGSTLA TQIEKYRHSP DGQTTGGVEK LRQMMSASIR
     AYRDGEDTTE ARRRVLVDYL NSTPLTARAG FGEVNGLGDG LWAWFGTDLS IAKRVLAEPA
     AEPRTLRLKA LAYKQVLALL LAQRRPSYYL IQDRTALDRL ADAHLRALAQ AGVIDPALRD
     AALAIRLAFR EEAPSPPATS FIEQKATNAV RARLLGMLGV PSLYQLDRLD LTAQSTLDAE
     TQARVVEVLG KLNDPDYART LGLTGERLLD ARNNDLSKLV YSITLYERGP EANYLRVQAD
     NLDQPLDINE GAKLDLGSTA KLRTLVTYLQ IVAELHSRYA HLPKDFLADV EDEASDNLTR
     WAASWLTTAQ DRRLPAMLDA AMERRYSANP GEVFFTGGGQ HSFVNFNKDD NGRIMTLQEA
     LRSSVNLPFI RLMRDIVQFY MDEGADDGAE ILRTPDHPAR QAYLARFADR EGSDFLNRFY
     NDYRKRTPDE ALVRLAARSR PVPYRLAVIF RTVRPKAGLA EFSAFLRARL PGSTLSDGEL
     SALYAKYGPG RFPLNDLGYL ARVHPLELWL VAHLQNNPNA TRAEVLAASA DERQESYRWL
     FKKGMAAQNT RIRIGLEEEA FKRITAQWRS VGYPFDTLVP SLATSIGSSA DRPAALAELM
     GLILNDGVRQ PTVRIRSLHF AAGTPYEAKL GLGPLKGERV LHPEVCATLR RALMDVAQNG
     TAKRVWGSFK DPAGTAVPMG GKTGTGDHRL ERWGPGGVLL ESKAVARTAT FVFYIGDRFF
     GTMTAFVQGP EADDYRFTSA LPAQLLKSLA PALQPLIDQG ATRTADTRPA PAGL
//
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