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Database: UniProt
Entry: A0A238U4M2_9FLAO
LinkDB: A0A238U4M2_9FLAO
Original site: A0A238U4M2_9FLAO 
ID   A0A238U4M2_9FLAO        Unreviewed;       763 AA.
AC   A0A238U4M2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=TJEJU_0170 {ECO:0000313|EMBL:SNR13976.1};
OS   Tenacibaculum jejuense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=584609 {ECO:0000313|EMBL:SNR13976.1, ECO:0000313|Proteomes:UP000215214};
RN   [1] {ECO:0000313|EMBL:SNR13976.1, ECO:0000313|Proteomes:UP000215214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=type strain: KCTC 22618 {ECO:0000313|Proteomes:UP000215214};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) 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}.
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DR   EMBL; LT899436; SNR13976.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238U4M2; -.
DR   KEGG; tje:TJEJU_0170; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000215214; Chromosome tjeju.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000215214};
KW   Transferase {ECO:0000313|EMBL:SNR13976.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..242
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          425..677
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          738..763
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   763 AA;  86656 MW;  101993F491B9D42D CRC64;
     MSEKKTISFR SYIKWFWGLL LGGILSICLV FLFASWGVLG KLPTFEQLEN PQNDLATEII
     SSDGKTIGKY YLKANRTPIK YKDLPDNLVK ALVATEDERF YEHSGIDFRG LARAIAKLGK
     GGGASTITQQ LAKNLFTKRA SSNKIKRIIQ KVKEWVIAVR LERQYTKKEI ITMYLNTQDF
     IFNAVGIRSA ARIYFGKEPK DLDLQESAII VAMLKNPRQF NPNRKISKKK SLNRRNVVFA
     QMLKNGFITQ QEKDSLQKLP LKIKFTPESH SDGLATYFRE HLKKFLKDWA KKNPKADGEL
     YDIYKDGLKV YVTIDSRMQQ YAEEAMTEHM SNLQKYFFAE HKKNKNAPFY DIERDDIRKI
     INRAKTNSDR YKRMKAAGKS DKEIEKAFNT KTDMTVFSWK GDRDTVMTPY DSIRYYKYFL
     RSGLVSIEPQ TGHIKAWVGG INNKHFKYEA VDQQKRQVGS TFKPFVYATA INQLKRSPCD
     KLPNTPYTIP KEKYGMDDDW TPKNAGNKYG GELTLQQALA KSVNVITARL IDEVSPINVA
     RLAKSAGIST EFQANPSIAL GAIDLTLLEM TSAYSTFANK GMRVTPIFIT QIEDKNGTVL
     ETFVPKTKEV LSEESAYVAL NLMEGVTKFG SGARLRSKYT RPKFITGYPY EFNNAIAGKT
     GTTQNQSDGW FMGTVPNLTT GVWTGGEDRS IHFVGLDKGG GASMSLPTWA IFMRKCYADK
     SLKISKADFE EPSDLSINVD CKKHEEKKDE KKDAEKVQNA DDF
//
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