ID G4T495_META2 Unreviewed; 788 AA.
AC G4T495;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:CCE24906.1};
GN OrderedLocusNames=MEALZ_3241 {ECO:0000313|EMBL:CCE24906.1};
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE24906.1, ECO:0000313|Proteomes:UP000008315};
RN [1] {ECO:0000313|Proteomes:UP000008315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC {ECO:0000313|Proteomes:UP000008315};
RX PubMed=22207753; DOI=10.1128/JB.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
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}.
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DR EMBL; FO082060; CCE24906.1; -; Genomic_DNA.
DR RefSeq; WP_014149664.1; NC_016112.1.
DR AlphaFoldDB; G4T495; -.
DR STRING; 1091494.MEALZ_3241; -.
DR KEGG; mah:MEALZ_3241; -.
DR PATRIC; fig|271065.3.peg.3335; -.
DR HOGENOM; CLU_006354_2_4_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008315; 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 Glycosyltransferase {ECO:0000313|EMBL:CCE24906.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCE24906.1};
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:UP000008315};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:CCE24906.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 334..422
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 424..696
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 788 AA; 88162 MW; 86E634FFBEC54EE1 CRC64;
MIIKLVITFF KWLSVLFLIG LISAAIYGYL LLERLSDELP DVNQLKDVHY QTPLQIYSKD
NLLIAEFGEK KRNPITIDQA PKELIHAFLA AEDKHFYEHH GVDFVGLFRA ALKLATTGKK
EQGGSTITMQ VTRNFLLSRE KTYTRKLKEI LLSLKIEETF SKDTILELYL NKIYLGQRSY
GVAAAAQTYY GKSLNELTLA ESAMIAGLPK APSAYNPIVN PARAMERRDY VLYRMHKIGY
IDQQTYQAAL AEANTARVIH RGIELSAPFI AEMARQKILE LYGTQAYGSG MKVYTTITRP
LQNAATRALR NAVHSYDERH GYRFKLPDAP AQKTDIDKMP IIGDSYPALI KRIDNDKATV
QLRGGKNVEV PWNNMKWARK FISRNARGAA PQSIHDLFKI GDAIFVRQLN DKTWALAQIP
EAEGAFVAID TIDGAILALA GGYDFNHNKF NRVTQSNRQP GSGFKPIIYT TALEKGYTAA
SLINDAPIVL EGSRPGHEWR PENYNRRFSG PTSLRVALRQ SKNLISVRLL LNLGIKPVVE
TAMRFGFQKN QLPNSYTLAL GSGQATPLQM ARAYAVFANG GFLIEPYLID RIESGDGKLL
YQANPQVACL DCTSESPSFI NQAPRIITPQ INFLMNSLLR DVVQRGTAVK AKRLGRTDLA
GKTGTTNDHR DAWFNGYSTT ISATAWVGFD NFNSLGYKET GGAAALPMWM EFMQAALQDK
PEIPLTPPEG VAKMYVDAES GMMMSAEIPG GIWEFFDTTQ QAHMHTNFEF TPPDEAHFSE
RHPIETLF
//
