ID A0A0C2F3X1_9PSED Unreviewed; 811 AA.
AC A0A0C2F3X1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=UCMB321_0542 {ECO:0000313|EMBL:KIH85723.1};
OS Pseudomonas batumici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=226910 {ECO:0000313|EMBL:KIH85723.1, ECO:0000313|Proteomes:UP000031535};
RN [1] {ECO:0000313|EMBL:KIH85723.1, ECO:0000313|Proteomes:UP000031535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCM B-321 {ECO:0000313|EMBL:KIH85723.1,
RC ECO:0000313|Proteomes:UP000031535};
RA Klochko V.V., Zelena L.B., Elena K.A., Reva O.N.;
RT "Complete genome of Pseudomonas batumici UCM B-321 producer of the batumin
RT antibiotic with strong antistaphilococcal and potential anticancer
RT activity.";
RL Submitted (JAN-2015) 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:KIH85723.1}.
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DR EMBL; JXDG01000004; KIH85723.1; -; Genomic_DNA.
DR RefSeq; WP_040063664.1; NZ_JXDG01000004.1.
DR AlphaFoldDB; A0A0C2F3X1; -.
DR STRING; 226910.UCMB321_0542; -.
DR PATRIC; fig|226910.6.peg.540; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000031535; 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 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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 317..420
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 425..701
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 783..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 88360 MW; 12AC60B889850870 CRC64;
MIRLLKFFGW SFVAVFCGLL LVLSGAFLYL SPGLPSVETL RSIQLQIPLR VYTSDGKLIA
EFGEMRRSPL RFADIPPNFI NALLSAEDDN FANHYGVDPS SLMRAATQLV KSGHIQSGGS
TITMQVAKNF FLSSERSFSR KTNEILLALQ IERQLTKDEI LELYVNKIYL GNRAYGIEAA
SQVYYGKSIR DITLAQMAMI AGLPKAPSRF NPLANPVRAK ERRDWILGRM YKLGKIDEAA
YQAAIVEPIN ASYHVPTPEV NAPYIAEMAR AEMVGRYGSD AYTEGFRVTT TVPSNLQELA
NHAVEEGLIT YDQRHGYRGP ESRLPGKTRD AWIAELGKQR TISGLDPAIV TQVDKTSLHV
LTRNGPEIVG WDSMKWARPY LNTNSLGAAP KQPADVAQVG DLIRVQRQAD NSLKFSQIPA
AQSALVSLDP QNGAIRALVG GFAFEQSNYN RATQAKRQPG SSFKPFIYSA ALDNGYTPAS
LVNDAPIVFV DEYLDKVWRP KNDTNTFLGP IRMREALYKS RNLVSIRLLQ SLGVDKTIDY
IAKFGFNKQD LPRNLSLALG TATLTPMEIA TGWSTFANGG YKIAPYLIEK IESRNGDTLF
VANPPSVPTG AAASSGIAVP SQPAFTVNNT SEAPAPAAQA PAVAEQIIDG RTTFILNSML
EDVIKLGTGR RALALGRGDL AGKTGTTNES KDAWFTGYNS DYITTVWTGF DQPESLGRRE
FGGTVALPIW MDYMGAALKG RPLHTQAEPE GILSLRVDPV SGRAATPGTP NAYFELFKSE
DTPPSVNEIG NGGSAPGSPL PADEAAPIDL F
//
