ID A0A1T4XEK7_9GAMM Unreviewed; 805 AA.
AC A0A1T4XEK7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-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=SAMN02745130_02893 {ECO:0000313|EMBL:SKA87899.1};
OS Thiothrix eikelboomii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thiothrix.
OX NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA87899.1, ECO:0000313|Proteomes:UP000190460};
RN [1] {ECO:0000313|EMBL:SKA87899.1, ECO:0000313|Proteomes:UP000190460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA87899.1,
RC ECO:0000313|Proteomes:UP000190460};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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; FUYB01000016; SKA87899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4XEK7; -.
DR STRING; 92487.SAMN02745130_02893; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000190460; 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: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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
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.
PE 3: Inferred from homology;
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:UP000190460};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..241
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..573
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 711..794
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 805 AA; 90962 MW; D7C73667F80F4264 CRC64;
MAQLPRLPLL PLSLARVQGR TLAKFCFSLL FLGGLLVGGW WWYFDSLPRP LFAKTHAQIL
LDRQGRLLSA HIADDGQWRF PAIEKVPDKF TIALTQFEDR RFQNHSGVDF LALIRATYDN
LRQQRIVSGA STLSMQVIRL ARGNPPRTLP EKIVEMFRAW RLESLYSKPE ILQLYASHAP
FGGNVVGLEA AAWRYFARDP EQLSWAEHAL LAVLPNNPAL IHPGRNRTQL LQKRNRLLAR
LYTVQVLSKL DYELAMAEPL PEAPHLLPRL APHLLDTLAA SYPQGERFQT TIDANLQQQL
VTLAQRTGDQ LALEGIQNLA ILVLDNHSLA TLAYIGNRPD RDYRAELGHA IDLIQRPRSS
GSTLKPLLFA DMLEQGMLLP DSLIADVPVN YTGFTPQNFN RQYHGAVSAR EALARSLNIP
FVNLLSLRGV DPFLMYLRQM GFQHLQRSAR HYGLSLVLGG AETSLWELTV AYANLAHLAQ
TSTIKQAYWQ QGRRLQTEIA DSGRIATLSK ATAWLTLDSL LDLARPGDEG YWDKFSSSRK
VAWKTGTSYG QRDAWAIGTT PDYTVGVWVG NANGEGRASL TGTQTAAPIL FNTFNFLPLG
RAWFSSPEAQ LTEVNICRND GYLSNGFCQT KRVKIPLGSH FSRMTPYHQR IYLDASQQWR
VNSECESISK MQARDWFVLP PDQAYYYKQY HADYQPLPPW RPDCVADLGH QQEALSVVYP
QEATQVYLPR ELDGKLGEVI FRAVPTHPEA LLYWHLDNQF LGTTQSFHQM AVQPAAGKHR
LAVVDESGQR IERQFEVLVH EDKSQ
//
