ID A0A1I6H9H4_9GAMM Unreviewed; 819 AA.
AC A0A1I6H9H4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN04488070_1642 {ECO:0000313|EMBL:SFR51145.1};
OS Pseudidiomarina maritima.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=519453 {ECO:0000313|EMBL:SFR51145.1, ECO:0000313|Proteomes:UP000199424};
RN [1] {ECO:0000313|Proteomes:UP000199424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7285 {ECO:0000313|Proteomes:UP000199424};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOYU01000002; SFR51145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6H9H4; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199424; 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 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 55..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 317..425
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 429..697
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 800..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 90429 MW; 15DFF0F8BEE905FC CRC64;
MKIFKWVLGV GVTLAILGSI AVVGLYFYWE DDLPSVAELK EVRLQTPMQV YSSDGEMIAQ
FGEIRRIPLQ LEEIPQPLIN AFLATEDQRF YDHFGIDPIG VARAFALLIS TGEIQGGGST
ITQQLARNFY LSFEQTWTRK IKEAFISLRM EKELTKDEIL ELYLNKITFG HRAHGVGAAA
QVYYGKDVQD LTLAQMAMIA GLPKAPSTMN PISNPERARE RRATVLGRML AENFISENQY
RDALAEPIET RLHGAEVTMS APYLAEMVRA DMVARYGEDA AYNSGFKVYT TVNAKQQRAA
QRAVQLNLHG YDERHGYRGA EQILWQPDEE AWEFDAIREF LRSQEAIGLT VPAVVLSVAE
KSAQVLTASG EPRELPWSGL AWARAYMHAD RQGPAPQAAT DILAPGQLVR IRATEQGLRL
AQVPEPSGAI ISLRPQDGSI AAAVGGYSFA VSQYNRAIQA KRQAGSNIKP FIYSAALENG
FTLATLVNDA PINQWNPGSG IAWRPRNSPD VYEGPIRVRQ GLAKSKNVVS VRLMRAMGID
TTVEYLTRFG FAIDELPRNE SLSLGSASMT PLEVARGYAV FANGGYLVNP YFIERIVDNN
DEVVYSARPA VACVLCEEER DVVQAPQVIS EQNAYLITEA MNSAVWGGGS WQHRTGWNGT
AWRIQRSKPI VDLAGRNIVG KTGTTNDVKD TWFSGFVSGL VTTAWVGFDN LERALGSTTM
NENLDSSEQP ISGTEAGAKT ALPMWIDYME TALEDATIEP FQVPPGLVMA RIDLATGKLS
RKNDYTTRFE YFLPGTAPTE YADSKSSSKD IFSDDDSIF
//
