ID A0A1Z4JLT4_LEPBY Unreviewed; 767 AA.
AC A0A1Z4JLT4;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 18-JUN-2025, entry version 30.
DE SubName: Full=Penicillin-binding protein 1C {ECO:0000313|EMBL:BAY57633.1};
GN ORFNames=NIES2135_45030 {ECO:0000313|EMBL:BAY57633.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Leptolyngbyales;
OC Leptolyngbyaceae; Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY57633.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY57633.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY57633.1,
RC ECO:0000313|Proteomes:UP000217895};
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=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
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DR EMBL; AP018203; BAY57633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4JLT4; -.
DR Proteomes; UP000217895; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000217895};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 65..232
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 314..558
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 667..746
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 767 AA; 85899 MW; F21CB680CDC2630F CRC64;
MRNRRFFSTK RRSYFTIVIV LILSGILLRS LPYLAPIRAS DIAQNDQAIE FQDRNGLPLG
SLLTRDQDHT AVISLNEVSP NLVQAILAAE DQGFYHHGAV DLKAGIRAIA EAIQARRIVS
GASTITMQLA RMLEPSPRTA WGKIQEIWLS WRLFAGMSKD EILQAYLNRL PMGGNIYGVE
AAARVYFGIP ARDLNLAQAS LLAALPNDPN DLNPYEHWEH LKKRQQYVLD RMVQDCYITQ
SQRDRIFAEA VKLQPRQQGI LAAPHFLFWS ANQLPKNHPA QIRTTLDLPL QQFVEAQARQ
VIETLARNNV HQAAAIVLDN RTGNVLAYVG SIDYFAASQM GQNDGVQALR QPGSTLKPFL
YQLALEKRII QPNTVLADVP THYAIPGAKL YSPTDYSETF QGPVRVRIAL ANSLNVPAVR
VLEKVGVAIF LDRLHQLGFA HLNQSPDYYG LGLTLGSGEV SLWELAQAYL LMARQGQSTL
LHPQSYSAYS TSTWSLITNM LSDRYARARS FGVDSVLSLP FPAAVKTGTS SDFRDTWTVG
FTTDYTVATW VGNFNGEPMR QVSGVTGAAP LWSRIMLHLH EHREPAALPL PKDLVQRPIC
ALSGLRPTAV CPTIVQEYFY PEDLTTYQQH PDTFYQAISN DQQQYRLNLP AEYNEWLAMQ
QEPILSPGTL RIISPRNGDY FLVAPERGSG QNLQFRLAEV PKQPVEWRLN GEKIATQTSN
TFFWNLRAGD WTLQARSGAS TDQVRFQVGV AEKPSTRRGF SLTEASR
//
