ID A0A418ZTH7_9RHOB Unreviewed; 850 AA.
AC A0A418ZTH7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=D3P06_13295 {ECO:0000313|EMBL:RJL00531.1};
OS Paracoccus aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=453842 {ECO:0000313|EMBL:RJL00531.1, ECO:0000313|Proteomes:UP000285530};
RN [1] {ECO:0000313|EMBL:RJL00531.1, ECO:0000313|Proteomes:UP000285530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19484 {ECO:0000313|EMBL:RJL00531.1,
RC ECO:0000313|Proteomes:UP000285530};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Laiz L.,
RA Saiz-Jimenez C.;
RT "Paracoccus onubensis nov. sp. a moderate halophilic bacterium isolated
RT from Gruta de las Maravillas (Aracena, Spain).";
RL Submitted (SEP-2018) 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:RJL00531.1}.
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DR EMBL; QZEV01000077; RJL00531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418ZTH7; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000285530; 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 Reference proteome {ECO:0000313|Proteomes:UP000285530};
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..235
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 329..451
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 453..742
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 523..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 93683 MW; 1C553890A4F6EF22 CRC64;
MLRPILSFFG AIFSWVVTAL VFAALTVGGV FWIYSRDLPS HETLAQYAPK TISRIYSAEG
QLIDEFAEER RIFVPIDEVP DLVKQAFISA EDKNFYSHPG YDLRGIGSAA YQALASRGAS
VRGASTITQQ VMKNFLLSSD RSVERKVKEL ILAARLERTL TKDQILELYL NEIFLGQNSF
GVVAAAQTYF NKSLSELAPH EAAMLAAMPQ APGRYHPVHA KDRVTERRNY VLREMWQNGF
IDQASYEAEA ALPLRSVQNG DFPSFRRSLP PRDYFTDEIR RQLSREFGQE EFFGGGLTIR
ATVDPDLQSQ AASALQQALE DYDRNRGIWR GTGEAIDPAA LSDEAAWRGA LWDLRLPRDI
PGWRPAVVLE VGPADARIGI EGIEETARGH WIPAADVQWA RPLDRETGRL GARAQVAGDL
VRPGDVVLVR AMTRDGDGGF IRWTLRQVPE VQGGFMAMDV NTGRVLAMQG GFSYESSVFN
RATQAQRQPG SSFKPFVYAA ALDNNYTPAT IVVDEPIRIN TPQGLWEPKN SSGRHYGPTP
LRTGIEQSRN LMTIRIADDI GMDQVARYAE KFGVYDRLSP FLANALGAQE TTLFKMVAAY
AMFANGGERV EPTLVDRVQD RRGRTVYRHD RRVCQTCAMQ ALPSGQAPAI DNNRERVMDA
VTAYQLTSML QGAVQRGSGS GVNLPVPIAG KTGTTNDAKD VWFIGYSSNI VAGCYLGFDQ
PRSLGERAFG GTLCVPVFNA FMREAVKEYG GTEFKVPPGG FWVKIDRLTG QRLPDSASGP
NVISEYFREG MDPDWLAPVI ISGFGEQVTI LPWEAGAGSG SGRAITTTTG ERRVIPARTD
FGTMSSGGLY
//
