ID C6ADR3_BARGA Unreviewed; 821 AA.
AC C6ADR3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 Name=mrcA2 {ECO:0000313|EMBL:ACS51318.1};
GN OrderedLocusNames=Bgr_10570 {ECO:0000313|EMBL:ACS51318.1};
OS Bartonella grahamii (strain as4aup).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS51318.1, ECO:0000313|Proteomes:UP000001489};
RN [1] {ECO:0000313|EMBL:ACS51318.1, ECO:0000313|Proteomes:UP000001489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT "Run-off replication of host-adaptability genes is associated with gene
RT transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL PLoS Genet. 5:E1000546-E1000546(2009).
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}.
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DR EMBL; CP001562; ACS51318.1; -; Genomic_DNA.
DR RefSeq; WP_015856373.1; NC_012846.1.
DR AlphaFoldDB; C6ADR3; -.
DR STRING; 634504.Bgr_10570; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; bgr:Bgr_10570; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_5; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001489; Chromosome.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 56..233
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 322..441
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 443..734
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 821 AA; 91159 MW; 7BE9EFE4874991AE CRC64;
MMIFLRYLLR FFVAIGLCGA ITWGVMTSGQ ANALPDYEVL SLYEPPVMTR VHASDGRLMA
EFATKHRLYL PIQSIPKLVI NAFISAEDKN FYHHFGLDPE GLSRALINNI RNIGSGRRPE
GASTITQQVA KNFLLSSETT LERKFKEAIL AMRIEKTYSK DHILELYLNE IYLGRGTYGI
AAASLTYFNK SVNDLTLEQC AYLAALPKGP ANYDPFKNTQ RAIDRRNWVI DRMIANGYVT
REQGEKAKAK PLGATIRGSD SYVFAADYFT EEVRRRLIHR YGAKTLYEGG LSIRTTLDPH
LQLIARRALH AGLIRFDHSQ GWRGAYAHID EKGDWGIELA NITGLSDVPE WRLAVVLSAN
PNKVEIGLQP QREASGILSK KREIAVLSES DSKWALHVVK ENGYRKTVQN LSHVLQVGDV
IFVEKLSNTN NTYRLQQIPK VEGAIVAMEP HTGRVLAMVG GFSFAASEFN RATQAYRQPG
SAFKPFVYAA ALDNGYTPAS VVLDGPIEVR QYNGEIWQPK NYGGTFAGPS TLRYGIERSR
NLMTIRLAND MGMPLVAEYA ERFGIVDKLQ PYLPMALGAG ETTVLRMVTA YSVIANGGRS
IKPSLIDRIQ DRYGKTIYRH DDRICENCNT PSWNNQREPT LIDERDQVLD PMTAYQITSM
MEGVVQRGTA ARLRYLNRHI AAKTGTTNDS KDVWFMGFTP DIVVGIFIGY DQPAPLGYNG
TGSSLAAPIF GEFMANALKG KPDVPFKMPK GMILMPINRK TGMLAERGDQ DVIIEAFKPG
TGPADIYQVI GSTNSFQEGV PAVTTSPQVN KALESGTGGL Y
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