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Database: UniProt
Entry: A0A1Q7IG66_9CHLR
LinkDB: A0A1Q7IG66_9CHLR
Original site: A0A1Q7IG66_9CHLR 
ID   A0A1Q7IG66_9CHLR        Unreviewed;       948 AA.
AC   A0A1Q7IG66;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-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=AUH89_00985 {ECO:0000313|EMBL:OLC62649.1};
OS   Ktedonobacter sp. 13_1_40CM_4_52_4.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805230 {ECO:0000313|EMBL:OLC62649.1, ECO:0000313|Proteomes:UP000186693};
RN   [1] {ECO:0000313|EMBL:OLC62649.1, ECO:0000313|Proteomes:UP000186693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLC62649.1}.
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DR   EMBL; MNFP01000019; OLC62649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7IG66; -.
DR   Proteomes; UP000186693; Unassembled WGS sequence.
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; 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   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   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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        172..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          243..452
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          566..846
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          38..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          927..948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..70
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  104415 MW;  C7F69326A71B33EB CRC64;
     MYDVPMSNDF WNQQYLNGHK PIEINGAARS VSILRDYRQQ PQQGQEVQQY APLSTPPPQG
     YSPYTPPPAP GQMYNNGEQQ GWPAPQSWPS ANNGQQQEQS WVANTLQKVR RWSGRIAAVP
     PVDPNPLVLY RPGKSWEQER PKTKPWKRSR TVRVAMLMKH RRVRWRQRRP KAGVIASGIL
     IALLLLLLIS ASASSAYAYK YYQDQLPRLQ GLANQQISQT SRIYDRNGTL LYEAYDNSHI
     GGGRRTPVSY NFLPQILKDA QISAEDPTFW TNPGIDPQAI LRASGQYLHA GAVVSGASTI
     TQQVIKNLTN NAAQTINRKI SEAALAIGLT QQYPKEKILE MYFNISPYGA QNLGVEAAVE
     DYFHISSQCD KNFNCTPGVY YLNCDAAHVQ QCHPEQCSQS NYCDPLLGLA RASLLAGMPQ
     SPAIYDPTFG LIDAATGQKY YLERQQYVLS QMLRWNVNVP GLGPITQDKV NQAEALTAKT
     QFPPYTHPYY HGCQHFVNWV IEQLTAQLGD AFFTGGFNIY TTIDYRLEAY VERAIKRHLQ
     KPELQLFPVA RVGVLSSPDY NVYDAAAVVM NAKTGEVLAM AGSANYNSKS SKIDGQFNSA
     VHALRQPGSS IKPIVYTTAF QQGWYPGMVI PDHKTYFPHG ISGSPAVCVG PTGAYCPQDY
     GGGYSNSNTN IRIATADSRN IPAIKASIYA GVGNVINMAQ RFGITAVSQN RDNNTSFALG
     TSGIPLIQMV GAYQVFADNG VRVPPRSILD IWDNYGHHLY HFDPAHPGGI QVISPQIAFL
     MTSVLSDEYA RRIEFWPDHD LSFWGNVNYP NPGYPNVAAK TGTTEDFKDN WTLGYTTRVV
     VGVWAGNADD SAMYNVAGIT GAAPIWHSVM TYVSGMCNSA NDGIPCPNTN LIFKPHTFTP
     PPGVVQACVS SSNGLAGNGN CDWMLDGEQP KSAGMVNPSN KPTPAPTP
//
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