ID A0A099LDY1_9GAMM Unreviewed; 857 AA.
AC A0A099LDY1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=ND16A_3082 {ECO:0000313|EMBL:KGK01075.1};
OS Thalassotalea sp. ND16A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassotalea.
OX NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGK01075.1, ECO:0000313|Proteomes:UP000029848};
RN [1] {ECO:0000313|EMBL:KGK01075.1, ECO:0000313|Proteomes:UP000029848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND16A {ECO:0000313|EMBL:KGK01075.1,
RC ECO:0000313|Proteomes:UP000029848};
RA Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA Hazen T.C.;
RT "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT Eastern Mediterranean Deep Water.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC from the lipid intermediates. The enzyme has a penicillin-insensitive
CC transglycosylase N-terminal domain (formation of linear glycan strands)
CC and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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 -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
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}.
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:KGK01075.1}.
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DR EMBL; JQDZ01000008; KGK01075.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099LDY1; -.
DR STRING; 1535422.ND16A_3082; -.
DR PATRIC; fig|1535422.3.peg.168; -.
DR eggNOG; COG5009; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029848; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; 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; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF17092; PCB_OB; 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 Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:KGK01075.1};
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:UP000029848};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:KGK01075.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 48..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 346..449
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 451..732
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 857 AA; 95050 MW; 25765A377383F530 CRC64;
MQLSLLGTAL LSLVIGGFYL SMRSELPSVE ILKDVQLQIP MQIYSNDGEL ISQFGTKRRI
PAKLADMPEQ LINAILATED NRFYEHFGVD PIGMTRAIIG QITGNDAGGA STITMQTARN
FFLTREQTYV RKIREIFISL HMESLLSKDE ILELYLNKIE LSHRAFGVGA AAQVYYGKEL
KQLTLAEIAV IAGLPKAPST YNPISNPDRA KFRRTTVLQR MLVSGYITEQ EYQQANNEDI
RTKRHGVDIE LDAPYVAEMA NKKALAMYGT EVAYGKGLKV YTTVQSELQQ AATAAVLGNI
HAYDERHGYR GAIKHLWLSE SDKELLTSRA ALSLNDNQFA QYKEQITKVS TQKPELEELV
KILKGVPLYN ELLPAIITNV DEQQAEILLK TGELAIIDWQ GMSWARAYVN DKSQGRAPKF
ANEIITAGDL IYVKAAEDNI FRLSQLPDVS GGLVAISPDS GAILASVGGY SFKQSQFNRI
TQANRQVGSN IKPFVYSAAL DNGYTLASIV NDAPINQWDR RSGFAWRPKN SPAVYEGPLR
VRTGLAKSKN VMSVRLLRGI KLKNLISHLA KFGFNSQELP KNESLALGSA SMTPLQVVTG
FSAFANQGYL VEPYIIDRIE DSNGEVIYQA EPQMACYQCE LAKAEYANSF ESIEDVDVEL
ITQAIAPRII SRENAFLVTE AMNSVIWGGG GDWSKGTGWS GTGWRAKTLN RRDLAGKTGT
TNQSKDAWFS GFSRRVAASS WIGFDDPARN LGRTVVNGNL GRNQTAGGEA GANAAQPSWI
KFMAVALNQY PYEAFEQPEN IVSIRIDKLT GKRTNKTDRS SRFEYFIQGT APKDWISDDN
IEEILESEEE TTEEELF
//
