ID A0A084CMZ0_9GAMM Unreviewed; 809 AA.
AC A0A084CMZ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KEY91169.1};
GN ORFNames=CF67_04185 {ECO:0000313|EMBL:KEY91169.1};
OS Candidatus Photodesmus blepharus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photodesmus.
OX NCBI_TaxID=1179155 {ECO:0000313|EMBL:KEY91169.1, ECO:0000313|Proteomes:UP000053784};
RN [1] {ECO:0000313|EMBL:KEY91169.1, ECO:0000313|Proteomes:UP000053784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ppalp.1 {ECO:0000313|EMBL:KEY91169.1,
RC ECO:0000313|Proteomes:UP000053784};
RA Hendry T.A., de Wet J.R., Dunlap P.V.;
RT "Selection and divergence in the genomes of co-occurring obligate luminous
RT symbionts with specific hosts.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KEY91169.1}.
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DR EMBL; JGVK01000027; KEY91169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084CMZ0; -.
DR STRING; 1179155.CF67_04185; -.
DR eggNOG; COG5009; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053784; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053784};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 41..215
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 302..419
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 423..689
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 809 AA; 91683 MW; BF2264232DD075C4 CRC64;
MTLSICAIFS FYYYERPKLP DVTALRDVTL QTPMQIFSQD GKLLSQFGEK RRIPITYSDI
PKYLIEALIA TEDSRFYKHF GVDPIGITRA VLVIIRSGSV REGASTITQQ LARNFFLSNE
KKILRKIKEI FIAMHIEQLL SKKEIMELYV NKIFLGHRSY GFAAAAQTYF GKDLQNLSLS
QIATLAGIPK APSTMNPIYS LERATNRRNL VLLRMLEEKY ITQQEYDKAR IEIVESRYHQ
SDIEVDAPYV AELARAWAVE LYGESAYTSG MNIYTTIDSK LQKAANQAAI DNLLAYDERH
GYRGAEKILW KVGQAAFTQQ QIENELKKTP VYGQIAPAIV TTVGSKSAKI WVKNSGEQTI
DWAGMSWARK FLTDEIQGPE PKYASDILHE GEKIWVRVKP TTNIQLKKSK VWLLSQIPNA
NTALVAINPE NGAILSLVGG FNFSYNKFNR ATQSLRQIGS SVKPFIYSAA IEQGMTLATL
INDAPINQWK KNQRVAWRPK NSPEIYSGPT RLRIGLAQSK NVMAVRVLRE VGLGKVRQYL
TRFGFNIDKL PHSETIALGA SSLTPIKMTQ AYSVFANGGY YIKPFYISKI EGPNGNLKFK
ANPKIICRQN CPEISLDNPT IHFAPQVISE QTAFLVREMM YSNIWGGGNW HDNSGWNGTG
WRAQNLKRHD IGGKTGTTNR SKDAWYSGYG PNIVTTVWVG FDDYNRSLGQ TKRSKKLDEQ
RISGIETGAK TAQPAWIKFM RIALQNQKTQ DKLLPPEIIR VRIDRKSGLL TNKFDANSMF
EYFLRGTEPR EYTETTNNIY NNSEVEELF
//