ID K9WIN7_9CYAN Unreviewed; 813 AA.
AC K9WIN7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 18-JUN-2025, entry version 58.
DE SubName: Full=Penicillin-binding protein 1C {ECO:0000313|EMBL:AFZ19661.1};
GN ORFNames=Mic7113_3954 {ECO:0000313|EMBL:AFZ19661.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19661.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ19661.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19661.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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; CP003630; AFZ19661.1; -; Genomic_DNA.
DR RefSeq; WP_015183798.1; NC_019738.1.
DR AlphaFoldDB; K9WIN7; -.
DR STRING; 1173027.Mic7113_3954; -.
DR KEGG; mic:Mic7113_3954; -.
DR PATRIC; fig|1173027.3.peg.4353; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_1_3; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000010471; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006793; P:phosphorus metabolic process; IEA:UniProtKB-ARBA.
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 InterPro; IPR001736; PLipase_D/transphosphatidylase.
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.
DR PROSITE; PS50035; PLD; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
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:UP000010471};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 317..348
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 813 AA; 90751 MW; F70F7E5222ED860F CRC64;
MRDYIRQKVW QRLSRSHRRF WKVTLVVVLL GLVVRSLPYL APIRAHDLVQ DQQAVEFSDR
NGLPLGTLLT RDQDHTAVLP IEQVSPPFIQ AILAAEDGRF YQHGALEMKA IARSILSSIH
AGRITSGAST ITMQLARMLE PAPRTLSAKL GEIWLSWRLA AGMSKQEILD AYINRLPMGG
NIYGVEAASR IYFGMSASEL NIAQASILAA IPNNPNYLNP YDYWEPLKRR QVYVLNRMVK
DGYITRQQAD RAYEEKISLQ SRQQGILAAP HFLFWVASQL PQSSIPHRMS QIRTTLDRPL
QQFVEAQVQQ IIRTLAPNNV HHAAALVIDN HTGEVLAYIG SPDYFLEAQL GRNDGVQALR
QPGSTLKPFV YELALENRII RPNTVLADVP TRYAIPGAKL YSPADYSETF QGPVRVRVAL
ANSLNIPAVR VLEKVGVPTF LQRLHQLGFA HLTHPPDYYG LGLTLGSGEV SLWELAHAYL
ILANQGQVKP LVTQINSPLI KQENNPKSLI GSATTWALIT DMLSDPHARA KAFGVDSVLN
LPFPVAVKTG TSSNYRDTWT VGFTTDYTVA TWVGNFDGEP MRQVSGVTGA APLWNRIMLH
LHEHQEPTAF SPPSGLVQRS VCALSGMRPT PACPSVVQEY FYPEDLGEYE RHPDTFYQGV
SSGSDGQPSQ YRLNLPEEYN EWLAMQPREA TLSSVSHTLP EGGKLSLSGN HLKIVSPRQG
DSFLLYPTES GAVQRLEFKL AATPTQPVEW WLNGEKLAMD SSNSLFWQLR PGNWTLEVRS
GDMSNRVSFQ VQLAENRATR RGFLIAPQGN HQR
//
