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Database: UniProt
Entry: A0A1H9IT13_9GAMM
LinkDB: A0A1H9IT13_9GAMM
Original site: A0A1H9IT13_9GAMM 
ID   A0A1H9IT13_9GAMM        Unreviewed;       682 AA.
AC   A0A1H9IT13;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN04488038_110166 {ECO:0000313|EMBL:SEQ77720.1};
OS   Solimonas aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Solimonas.
OX   NCBI_TaxID=489703 {ECO:0000313|EMBL:SEQ77720.1, ECO:0000313|Proteomes:UP000199233};
RN   [1] {ECO:0000313|EMBL:SEQ77720.1, ECO:0000313|Proteomes:UP000199233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25927 {ECO:0000313|EMBL:SEQ77720.1,
RC   ECO:0000313|Proteomes:UP000199233};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR   EMBL; FOFS01000010; SEQ77720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9IT13; -.
DR   STRING; 489703.SAMN04488038_110166; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000199233; Unassembled WGS sequence.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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:SF15; PENICILLIN-BINDING PROTEIN 1C; 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   3: Inferred from homology;
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:UP000199233}.
FT   DOMAIN          69..225
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          299..538
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   682 AA;  75466 MW;  EB1EF300370BBB76 CRC64;
     MKARLLRGVK WGALAALSLL MLATLLSQRA LPERLQPSLQ GAPPQILDRE GQPLHSVYDG
     GLNLYEQRAL EAMPLALRQA FVEAEDRRFW RHSGVDWRAR AMALRVNLRA GRALRGASTI
     SEQVVRILNP RPRTLWSRWV EGFEAWRLEA RFNKSEILEF YLNQVPYGGN RRGVVQAADY
     YFARSLDTLS QDEMLALAVL VRAPSRLARE PQALLKRVQQ LAQRLQLPPP QDLLALQRRS
     APLEAAYFLA QLERELATQV PQRASLRSSL DSGLQADTER YLAERLQELS REGAQQAAAL
     VVDLDGNRVR AYAAADARAP QAIGIDPLQV PRQPGSTLKP LLYALSLEQG WRADTVIEDA
     TLRERVNEGL HEYRNYSRQH YGAVTLAEAL GNSLNIPAVK ALQFVGQERF LSRLQDLGVR
     SLRQSAAFYG DGLALGNGEL SLFELVQAYT ALAREGLWQP LSLREDGEAP LPRRLIRPEA
     ARAISGILAD ADSRRLEFGD GSLLSFAQRT AVKTGTSSDY RDAWTIAYNG RYLLGIWVGN
     LSGRATQGVT GARGPALLAR SLLARLPEAG ALRAAPPPSA LARAAPAAEP QAEDPVLLQP
     FEGLLMARDP RIPETLQAFR FELGWRQPLR SVRWELDGEF LAQTADKFLD WPLSAGVHRL
     RAVATAASGA SAATPEVSFR VR
//
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