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Database: UniProt
Entry: E6X864_CELAD
LinkDB: E6X864_CELAD
Original site: E6X864_CELAD 
ID   E6X864_CELAD            Unreviewed;       748 AA.
AC   E6X864;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   OrderedLocusNames=Celal_2400 {ECO:0000313|EMBL:ADV49690.1};
OS   Cellulophaga algicola (strain DSM 14237 / IC166 / ACAM 630).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=688270 {ECO:0000313|EMBL:ADV49690.1, ECO:0000313|Proteomes:UP000008634};
RN   [1] {ECO:0000313|EMBL:ADV49690.1, ECO:0000313|Proteomes:UP000008634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14237 / IC166 / ACAM 630
RC   {ECO:0000313|Proteomes:UP000008634};
RX   PubMed=21475589; DOI=10.4056/sigs.1543845;
RA   Abt B., Lu M., Misra M., Han C., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Brambilla E., Rohde M., Tindall B.J., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Cellulophaga algicola type strain (IC166).";
RL   Stand. Genomic Sci. 4:72-80(2010).
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; CP002453; ADV49690.1; -; Genomic_DNA.
DR   RefSeq; WP_013551164.1; NC_014934.1.
DR   AlphaFoldDB; E6X864; -.
DR   STRING; 688270.Celal_2400; -.
DR   KEGG; cao:Celal_2400; -.
DR   eggNOG; COG5009; Bacteria.
DR   HOGENOM; CLU_006354_2_4_10; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000008634; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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   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   Glycosyltransferase {ECO:0000313|EMBL:ADV49690.1};
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   Transferase {ECO:0000313|EMBL:ADV49690.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..242
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          439..655
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   748 AA;  84474 MW;  3215D8B69B30F132 CRC64;
     MIFKKIKSPI LRYLLIAILS VFLFFILFIG SIQIGLWGSL PSKKELSNLE YQKASEVYAA
     DSTLIGKYYL FDRQPIAFEE FPENLLDALI AIEDERFYTH SGVDYPSLMR VAFKSILMQD
     QSSGGGSTIT QQLAKNLYPR EERKKTNIAV DKIKEMFIAS RLEDLYSKEE LLYHYLNTVS
     FGDNTFGVES ASLKFFNKKA KNLNTEEAAV LVGMLKATYG YNPRVFPENS LKRRNLVLQA
     MQKNNYLSEK QKDSLTALPL KLDYKEFNYN DGLAPYFREE VRKQLLAWSA TQKENGQEYN
     IYTSGLKIYT TLDYKMQQLA EEAMVAHLTV LQKDFEKSYG KNAPWLTNKK LLDKLLKRTS
     AYKRLKKNGL SEGQILDSLS IKRKMMLADW ESEKTVEAST LDSLQHYLKY LNTGSLGIDP
     TSGAVKTWIG GVNFKYFKYD HISQSKRQVG STFKPIVYTA ALENGLAPCT YFSAQEVAYE
     NLKGWSPSNS GNKDEAYLNY SMEQALSNSV NTVAVKVLEE VGVLKVIRQA NKMGILEKLP
     SEPSLALGTG EIKITELAGA YASFVNNSKP VTPYLIQTIS NSKDSILETF KPKVAEVEAF
     SSETRQTMIE MMKETINSGT ASRLRDTYNL PNAIAGKTGT TQNNKDAWFV GVTPKLVHIT
     WVGLDNHELG FKSTSLGQGA NAALPMFALL MQKLNKDKEF NAITKAQFET PSDKVLENLS
     CDPIKKDGFL KRLFKNPEKK KTKKFKSN
//
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