ID A0A061QFJ6_9PROT Unreviewed; 826 AA.
AC A0A061QFJ6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=mrcA {ECO:0000313|EMBL:GAK33037.1};
GN ORFNames=AQ1_00920 {ECO:0000313|EMBL:GAK33037.1};
OS alpha proteobacterium Q-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK33037.1, ECO:0000313|Proteomes:UP000027360};
RN [1] {ECO:0000313|EMBL:GAK33037.1, ECO:0000313|Proteomes:UP000027360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK33037.1,
RC ECO:0000313|Proteomes:UP000027360};
RX PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT "Iodide oxidation by a novel multicopper oxidase from the
RT alphaproteobacterium strain Q-1.";
RL Appl. Environ. Microbiol. 78:3941-3949(2012).
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:GAK33037.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAYV01000010; GAK33037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061QFJ6; -.
DR STRING; 1492281.AQ1_00920; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000027360; 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 Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..241
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 328..455
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 457..749
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 826 AA; 90492 MW; AB6E2002B4EC4D13 CRC64;
MSRRKRIVVW CLAGFGGMAL FSGLLLAGGV IYALLVYGRD LPDYRQLADY EPPVMTRVHA
GDGSVLAEFA TEKRLFIPIE VIPKRVVHAF LSAEDKNFYQ HPGLDFMGIA RAMVMNVRNV
FVGRRPVGAS TITQQVAKNF LLTNEVSYER KIKEAILAFR IEKAFSKDRI LELYLNEILF
GYGSYGLAAA ALNYFDKSVD ELTLAESAYL AALPKAPYNY HPIRRKEAAI GRRNWVLGQM
QENGYISKDA MQTAQAQPLD VRPRSAAANF RADYYEEAVR RHLARDYGTD ELYGGGLSVR
TSLEPRLQAI AEKAMHDGLI AYDRRHGWRG PITQRSIEGD WPSRLAAVPT MLGMADWQMA
LVHDVRAAGA VIGLVDGSYG FIPFDEMRWA RRWLPGERVS QSPDDPADVL SIGDVIAVEP
LPDQEKKTVL DRFVTDAGEP VGAVGSYALR QIPAVEGALV ALDPHTGRVL AMVGGFDFAA
SQFNRATQAE RQPGSAFKPF VYAAALEEGF TPSSLVLDAP FVIDQGEGQG KWKPRNSSNR
FYGPSTLRLG LEKSRNLMTI RVAQFIGMDK VLGLANRFGL AQGMEPNLAH ALGAGEVTPI
DLTAAYAMLV NGGKKIEPSL IDRIQDRYGK TIMRNDQRDC PQCDATEWHN QAPPTLPDHR
PQIIDPRIAY QVVHMLEGVV ERGTGRRIRS VGIPLAGKTG TTNESFDAWF VGFAPDLAVG
VFVGFDQPRS LGPGEEGSSA AAPIFRDFMA KAFEGEQGIP FRIPQGVRLV RVDAQTGVPA
RLGDQDVILE AFIPGTEPSG GDIAVLDGPG SLALDGRLRK GTGGLY
//
