ID F9T1K0_9VIBR Unreviewed; 839 AA.
AC F9T1K0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-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 ORFNames=IX91_14190 {ECO:0000313|EMBL:AIW15284.1};
OS Vibrio tubiashii ATCC 19109.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW15284.1, ECO:0000313|Proteomes:UP000030071};
RN [1] {ECO:0000313|EMBL:AIW15284.1, ECO:0000313|Proteomes:UP000030071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW15284.1,
RC ECO:0000313|Proteomes:UP000030071};
RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT tubiashii.";
RL Submitted (AUG-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}.
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DR EMBL; CP009354; AIW15284.1; -; Genomic_DNA.
DR RefSeq; WP_004743295.1; NZ_CP009354.1.
DR AlphaFoldDB; F9T1K0; -.
DR STRING; 1051646.IX91_14190; -.
DR KEGG; vtu:IX91_14190; -.
DR PATRIC; fig|1051646.9.peg.2775; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000030071; Chromosome 1.
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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 317..434
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 438..711
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 839 AA; 93460 MW; 780380A9D62250A8 CRC64;
MKFIKRLLIF TLICIILGVG TIFGFYLYVK PELPDVATLK DVKLQTPMQV FSQDGKLISQ
FGEKRRIPVA YDDIPQHLIE ALIATEDSRF YDHPGIDPIG ITRAAVVVAL SGSAKQGAST
ITQQLARNFF LSNEKKIMRK IKEIFIAIHI EQLLSKEEIM ELYVNKIFLG YRSYGFGAAA
QTYFGKELQN LTLSEIATLA GMPKAPSTMN PIYSLERATN RRNVVLLRML DEKYITQAEY
DEARGEEIVA RYHGAEIELS APYVAELARA WMVARYGQEE AYTSGMNIYT TVDSKLQAAA
NKSAINNLLA YDERHGYRGA EKVLWQPGKP ALDEQKIDKT LDNVPTYGQL VPAVVTKVDS
KQATIWVKDQ GINTLEWDGI KWARKFLTDD RQGPPPSNAK DVLAEGEQIW VREVESTVEG
QEPTIAWHLS QVPNANTAFV AMNPENGAVL SLVGGFNFVH NKFNRATQSV RQVGSSIKPF
IYAAAIDKGL TLATLINDAP INQWDKSQGT AWRPKNSPPT YIGPTRLRIG LAQSKNVMAV
RVLREVGLDE TRQYLTRFGF DIDQVPRSET IALGAGSLTP MKMAQGYSVF ANGGYYVEPF
YISRVEGPFG DLEFEASPKV VCHQDCTQAV TSDNEFAEQD VTTEVTEEPQ YAPQVISEQT
AFLMREMMYS NVWGGGNWRD GTGWNGTGWR AQKLQRRDIG GKTGTTNDSK DAWYNGYGPG
MVAIAWVGFD DHTRKLGRTK TNSNLGKDQI TGAEAGAKTA QPAWVDFMRT ALAGVPQQSK
TIPQNIVRVR IDRDSGLLTN KFDSSSMFEY FLEGTEPTEY VTSEITDSIY TSDGGEELF
//
