ID A0A0X3U1Y7_9RHOB Unreviewed; 828 AA.
AC A0A0X3U1Y7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=AVO44_02145 {ECO:0000313|EMBL:KUJ82095.1};
OS Ruegeria profundi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ82095.1, ECO:0000313|Proteomes:UP000053690};
RN [1] {ECO:0000313|Proteomes:UP000053690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT108 {ECO:0000313|Proteomes:UP000053690};
RA Zhang G., Stingl U.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:KUJ82095.1}.
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DR EMBL; LQBP01000001; KUJ82095.1; -; Genomic_DNA.
DR RefSeq; WP_068331856.1; NZ_LQBP01000001.1.
DR AlphaFoldDB; A0A0X3U1Y7; -.
DR STRING; 1685378.AVO44_02145; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053690; 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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 329..432
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 434..724
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 798..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 828 AA; 91677 MW; 45678A85CBF45DB7 CRC64;
MIRFILSFFG AIFSLVTLGI FMAALVIGAI FWMYGRDLPS HESLAQYKPP TISRIYSGKG
QLIDEFAQER RLFTPSEEIP DLVKQAFISA EDKNFYTHQG YDPRGIIAAG VEAVKSKGEN
VRGASTITQQ VMKNFLLSGD RRAERKIKEI ILATRLEDTL DKEQILELYM NEIFLGQNSY
GVTAAAQTYF NKTLQELEPH EAATLAAMPK APSDYHPVRQ KDRLLARRNY VLREMQQNGY
IDQATYEHEV AQPLRSVQNG DFESFRTALP PRDYFTDEIR RQLSEDFGEG EFFTGGFTVR
ASVDEEMQVE AAKALRTALQ KYDRSRGRWR GTGEVIPEEK LADETQWREA LAIMEIPRDV
VLPTQWYPAV VLNVAEQSLT VGIEDGPADG VIPRSDISWM QGDFAANFKR GDVILVMAGE
EGQWSARQVP EVQGGFVAMD VNSGRVLAMQ GGFSYQDSVF NRATQAQRQP GSSFKPFVYA
AALDSGYSPA TIVVDAPIEV NTPQGLWRPK NSTNKFYGPT PLRTGIEQSR NLMTIRLAQE
VTMPVVAGYA ERFGVYDRMG AFLANSLGAE ETTLYKMVAA YAMFANGGER VEPTLVDRIQ
DRFGKTIYRH DDRQCVDCNS GWLEPDESPT IVTDRWQVMD AITAYQLTSM MKGVVDRGTA
SSVVNLPVPT AGKTGTTNES KDAWFIGFTS NIVAGCYIGY DRPRPMGRGA YGGTLCGPVF
QSFMEKAVEK YGGGPFEVPP GGQFIKIDRF SGARLPEDAT GDYVVAEYFR DGVDGFIDRV
YDGGFAMGSD LPLFEEASSG RQVTTSTGST VTVGPNASQG DLQGGGLY
//
