ID F9H9Y2_STRMT Unreviewed; 727 AA.
AC F9H9Y2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpA {ECO:0000313|EMBL:EGP70010.1};
GN ORFNames=HMPREF9958_0294 {ECO:0000313|EMBL:EGP70010.1};
OS Streptococcus mitis SK1073.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1008452 {ECO:0000313|EMBL:EGP70010.1, ECO:0000313|Proteomes:UP000003815};
RN [1] {ECO:0000313|EMBL:EGP70010.1, ECO:0000313|Proteomes:UP000003815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1073 {ECO:0000313|EMBL:EGP70010.1,
RC ECO:0000313|Proteomes:UP000003815};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (MAY-2011) 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 -!- 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:EGP70010.1}.
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DR EMBL; AFQT01000019; EGP70010.1; -; Genomic_DNA.
DR RefSeq; WP_001041322.1; NZ_AFQT01000019.1.
DR AlphaFoldDB; F9H9Y2; -.
DR PATRIC; fig|1008452.3.peg.451; -.
DR Proteomes; UP000003815; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR NCBIfam; NF038272; strep_PBP1A; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 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 Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 333..602
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 658..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 80594 MW; 48B485D9CFBE37F6 CRC64;
MNKQIILRFL KYMGITFLTL FIALFLLGGG VFLYFVSKAP ALSESKLVAT TSSKIYDNKN
ELIADLGSER RVNAQANEIP TDLVKAIVSI EDHRFFDHRG VDTIRIMGAA LRNLQGKGGL
QGASTLTQQL IKLTYFSTST ADQTLSRKAQ EAWLAVQLEQ KATKQEILTY YINKVYMSNG
NYGMQTAAEN YYGKDLKDLS LPQLALLAGM PQAPNQYDPY SHPEAALERR NLVLSEMKGQ
KYISAEDYEK AINTPITDGL QSLKSANSYP AYMDNYLKEV IDQVEQETGY NLLTTGMEVY
TNVDKDVQQR LWDVYNTDEY VAYPDDELQV ASTIVDVTNG KVIAQLGARH QSSNVSFGIN
QAVETNRDWG STMKPITDYA PALEYGVYDS TASIVHDVPY NYPGTDTPVY NWDHGYFGNI
TIQYALQQSR NVTAVETLNK VGLDRAKTFL NGLGIDYPSI HYANAISSNT TESNKQYGAS
SEKMAAAYAA FANGGTYHKP MYINKIVFSD GSEKEFSDAG TRAMKETTAY MMTEMMKTVL
AYGTGRGAYL PWLPQAGKTG TSNYTDDEIE KYIKNTGYVA PDEMFVGYTR KYSMAVWTGY
SNRLTPIVGD GFLVAAKVYR SMISYLSEDD QPGDWTMPDG LFRNGEFVFQ NNAKNTWNNS
VTQQTQTVET PSTTAESSTT QASTTAGQQP NNAPATDPNQ GQAGQAGQPT QPVQPTPQNP
QVQQPQQ
//
