ID Q60BY9_METCA Unreviewed; 830 AA.
AC Q60BY9;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
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:AAU90416.1};
GN OrderedLocusNames=MCA0324 {ECO:0000313|EMBL:AAU90416.1};
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU90416.1, ECO:0000313|Proteomes:UP000006821};
RN [1] {ECO:0000313|EMBL:AAU90416.1, ECO:0000313|Proteomes:UP000006821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC {ECO:0000313|Proteomes:UP000006821};
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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}.
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; AE017282; AAU90416.1; -; Genomic_DNA.
DR AlphaFoldDB; Q60BY9; -.
DR STRING; 243233.MCA0324; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; mca:MCA0324; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; ISS:JCVI.
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; ISS:JCVI.
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:UP000006821};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..239
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 326..434
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 436..691
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 768..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 830 AA; 91603 MW; 66E31C24F71BC2F8 CRC64;
MAIFSRKTRR PRYWLMTLEV LLVAILVIAL GLFGLYRHLE PQLPDIAILK EVRYQIPMSV
YSRDGKLIAQ FGEKKRSPVA IGSVPQDLIH AFIAAEDDRF YDHVGVDYQG ILRAVLTFAR
TGEKRQGGST ITMQVARNFF LSSEKTFLRK IKEIMLAIRI DSELSKDQIL ELYLNKIYFG
QHAYGIEAAA QVYYGKHVGE LTLGEMAMIA GLPKAPSAFN PVANPERAQT RRNYVLRRMR
KLRFITDEVY QRALNEPITA RIHTRLIELD APYVAEMVRA EMYQQYGDDA YESGYAVYTT
IDSHAQRTAE SALQSGLRAY DERHGYRKAK VHIDLKQLKA KSAWNQILED QGPAGDTVPA
LVLTATDTTA GLYTVNHGEP ELSYDAVRWA RPFISVDAHG VPPRSVKEVL KPGDVIRIRK
NADGRWVLTQ IPKVQGALVE LDADSGAIIA VAGGFDYRLS KFNRASQGQR QPGSGFKPVV
YSAALDSGFT PASVVNDSPV SFPDPASPGG IWRPHNYSMK YAGPTPLREA LAKSRNMVSI
RLLRAVGLPK VIELAEKFGF TPDELPRSYT LALGSGTASP LRMAQVYAVF ANGGYRVDPY
LISRIETQNG RLLYQATPAI ACLDCADGKS TANRAKRVIS EEVHYMMHSM LQDVVRRGTA
TKALELGRSD LAGKTGTTNQ YRDAWFNGYV PGLVTVAWVG FDSYQTLGDK ETGGQTALPI
WMEFMKEMLR DVPERKFPQP AGIMAARIDP ATGNRLPASV PGGIVELVPR PTPQPGFDAA
AEEPEVAAPA SQSDASGARA PESIPPEEEE IGEAPPAQPA ETPKPMESLF
//
