ID F7S152_9GAMM Unreviewed; 871 AA.
AC F7S152;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 ORFNames=A28LD_2266 {ECO:0000313|EMBL:EGN74239.1};
OS Idiomarina sp. A28L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=1036674 {ECO:0000313|EMBL:EGN74239.1, ECO:0000313|Proteomes:UP000053031};
RN [1] {ECO:0000313|EMBL:EGN74239.1, ECO:0000313|Proteomes:UP000053031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A28L {ECO:0000313|EMBL:EGN74239.1,
RC ECO:0000313|Proteomes:UP000053031};
RX PubMed=21742887; DOI=10.1128/JB.05648-11;
RA Gupta H.K., Singh A., Sharma R.;
RT "Genome Sequence of Idiomarina sp. Strain A28L, Isolated from Pangong Lake,
RT India.";
RL J. Bacteriol. 193:5875-5876(2011).
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:EGN74239.1}.
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; AFPO01000026; EGN74239.1; -; Genomic_DNA.
DR AlphaFoldDB; F7S152; -.
DR STRING; 1036674.A28LD_2266; -.
DR PATRIC; fig|1036674.4.peg.2248; -.
DR eggNOG; COG5009; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053031; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000053031};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..242
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 365..465
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 470..751
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 851..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 97979 MW; 57370789CF020407 CRC64;
MRLFYLGDGG NSVIRFLKYF LLTIVALIFL GFATVAGLYY YVKDDLPSVD TLRDVRFLTP
MQVYTADGKL MSQFGEQRRI PLTLDEIPQS MIDAILATED SRFYSHRGVD PIGVMRAFWV
LVSTGEIREG ASTITMQLAR NFFLTRERVW IRKIKEAFIA LHIEQLLSKD EILELYLNKL
ELGHRAFGVG AAAQVYYGRD LDQLDLSEIA TLAGMPQGPS ILNPISNPAA SVQRRRIVLG
RMLAENYITR DEYDVAFRAP VSARYHVAEL ELNAPFLAEM VRQEMIQRFG VDDAYNGGYK
VHTTVNSEQQ LAAEYALREN LHAYDERHGY RGPEMRLWGI DPESLFSDSK TQLQKLPDEA
TLATMMQNRG EQWPEADIIQ YLERQPRFGR LQHAIVSDVH EKTADVILRG GMRATIEWNQ
MDWARRYIDA ERQGFAPKSA SEILNRGDHV LLRPVEEGYR LAQMPGPGSA IVALNPNNGA
LQSIVGGYSF NHSQFNRANQ AKRQVGSSIK PFIYAAALDR DFTLATLVND APVTQWNPGS
GSAWRPRNSP EVYDGPIRLR EALARSKNVV SVRLIRELGV NQTADYIERF GFLPNDVQRN
ESLSLGAASF TPLEMARGFA VFANGGYLVT PYFIDRIEDS DGNIIFQSQP EYACARCAAE
AVGIEFTNDD YANEAILSER NQAPRVIPEQ VAYLVTEALQ SAVWGGGSWA NQTGWNGTAW
RAQALRNRNL AGKTGTTNDV KDTWFVGYTR DIVAASWVGF DNLEFALGRT SLNSNLGRQR
QPIVGSEAGA TTALPGWVTY MQTALSQLEE RPFELPPNMV SVRIDQPSGR LTNRTDHTSM
FEYFIRGTEP KEFANPDRRP QEVFEDEEGL F
//
