ID A0A0S8EUL3_9GAMM Unreviewed; 808 AA.
AC A0A0S8EUL3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=AMJ59_27060 {ECO:0000313|EMBL:KPK52243.1};
OS Gammaproteobacteria bacterium SG8_31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK52243.1, ECO:0000313|Proteomes:UP000051321};
RN [1] {ECO:0000313|EMBL:KPK52243.1, ECO:0000313|Proteomes:UP000051321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_31 {ECO:0000313|EMBL:KPK52243.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK52243.1}.
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DR EMBL; LJTI01000228; KPK52243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EUL3; -.
DR PATRIC; fig|1703405.3.peg.2924; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051321; 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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..233
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 320..425
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 428..702
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 782..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 808 AA; 88909 MW; 706EC92DE00835D8 CRC64;
MTLLFRTLYA AAILVLALIA IVGIAAIGAY YYVAPSLPAV DSLKQVQLQV PLRVYTRDGL
LLAEYGEQRR IPLEFRDIPD VIQEAFLAAE DDRFYHHPGV DYQGLLRATF ALAVTGERAQ
GGGTITMQVA RNFFLTREKT ISRKVREIFL ALRIERQLSK QEILTLYLNK IFLGQRAYGV
GAAAEVYFGK SVHDLTLAEA ATIAGLPKAP SRDNPVSSPD RALSRRAYVL RRMLETGYID
QASFQQANAE PMKSMVHGPT VEVDAPYVGE MARQYMLERY GPEAYTAGYQ VTTTVDSRLQ
VHALSALRKG LIEYDRRHGY RGPLAIVDWP TEDGDPESIL SAVRTSPGMR PALVTAVDET
GARVTLNDGE QIVLDLEAVK WARPYIEVNL RGPAPEAVAD VLSPGQIVEL LRTADGGWSL
GQTPDAQGAI VALDPIDGAV VALAGGFDFQ ASKYNRATQA KRQPGSSFKP FIYSAALENG
FTAASIVNDA PVVFEDATLE DTWRPENYSQ RFYGPTRLRE ALVRSRNLVS IRVLRSTGVG
PAIRHIRDFG IPESIMPRDL SLALGSINLA PLDIAAAYTV FANGGYRVPA YFIQSVRNSV
GEVIEEADPL VACATCEDRA LEQEERDREA GFGSEDEPEP NLVAVEYAEP VISRQNAYLI
ADMMRDVIRR GTGRRAMSLG RSDLSGKTGT TNERRDAWFS GFNADLVATV WVGFDEEQSL
GAREEGSRTA LPIWIDFMGD ALKGMPERIP PKPSGLVTVR ISPETGRVAR ANDGDAIFET
FRVDHVPERD EEDAPSPYEP EEQTEPLF
//
