ID A0A1Z4NJT2_9CYAN Unreviewed; 850 AA.
AC A0A1Z4NJT2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=NIES3974_26210 {ECO:0000313|EMBL:BAZ05964.1};
OS Calothrix sp. NIES-3974.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005462 {ECO:0000313|EMBL:BAZ05964.1, ECO:0000313|Proteomes:UP000218621};
RN [1] {ECO:0000313|EMBL:BAZ05964.1, ECO:0000313|Proteomes:UP000218621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3974 {ECO:0000313|EMBL:BAZ05964.1,
RC ECO:0000313|Proteomes:UP000218621};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; AP018254; BAZ05964.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4NJT2; -.
DR OrthoDB; 499624at2; -.
DR Proteomes; UP000218621; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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 InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000218621}.
FT DOMAIN 131..304
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 396..640
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 94745 MW; BDADE2D155BD10D8 CRC64;
MVKFNSWFQD KSVPITDRDT QNENPEFSTN TELIPDTDTN TGDTATDDQP PPSKSVWKRM
GSVLSAVINK LPGHPKPLYQ RRWFWTWLGL GGSAAAISYG IWSIDQQLPP TAELNSIARE
QTLTIKGADG SILRQTGPAT RDRLSISQIP EKLRQAFIAS EDRRFTQHDG VDYQGIVRAV
VNNVRSQGVV EGGSTITQQL SRILFLKQEK TVVRKLREIR LAQKMERELT KDEILERYLN
LVYLGAGAYG VADAAWVYFS KSVDELTLAE MATIAGLAPA PSIYAPDRNP SAAKVRRNLV
LQRMLEDGYI TPSEREAAAS EELVLKPSLP KRTQITAPYF TSYIEKELPK LVPQDVLAAG
GLTVETTLDP KWQEYAEAAV NKTIRNRGRW ERFQQGALVS LNPRTGEIKA MVGGKDFDKN
QFNRVTQAQR QPGSTFKAFV YAAAIASGQS PYDTYVDAPY VVDGYEPKNF DEGFRGSMDI
RNALTKSVNI IAVKALVRTG FNPIIKLAQD MGIKSTLKPT YSLALGSNEV NLLELTSAYG
SFANEGLHTE AHGISRILNR QGNVLWQAQY QPRRVLDSDS AAIMTWMLRS VVTSGTGSPA
SLDRRAVAGK TGTTDKARDL WFVGYIPQVV TGVWLGNDNN RPTHGSSATA AYTWQQFMSK
ATADLPIEKF PELPKLQGRK ASIKAEPVRP IRVVNRPIST DNQVDTNDDA EVPRRRRRRR
HDSINSEVNV EVNENRSSRR RRRRNQQSSE NSSVTAEVTT EQNQRPRRRR RRIDRNMDDS
NQSSQSSQST ENSSPSRSRR RRRNSNPEST SPQPRRRSSA PASSGSSSGT GSSEGSSPSW
RERLRPSGGE
//
