ID A0A246JZ38_9SPHN Unreviewed; 838 AA.
AC A0A246JZ38;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=CDQ91_07220 {ECO:0000313|EMBL:OWQ98293.1};
OS Sphingopyxis witflariensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=173675 {ECO:0000313|EMBL:OWQ98293.1, ECO:0000313|Proteomes:UP000197097};
RN [1] {ECO:0000313|EMBL:OWQ98293.1, ECO:0000313|Proteomes:UP000197097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14551 {ECO:0000313|EMBL:OWQ98293.1,
RC ECO:0000313|Proteomes:UP000197097};
RX PubMed=12508864; DOI=10.1099/ijs.0.02217-0;
RA Kampfer P., Witzenberger R., Denner E.B., Busse H.J., Neef A.;
RT "Sphingopyxis witflariensis sp. nov., isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 52:2029-2034(2002).
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:OWQ98293.1}.
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DR EMBL; NISJ01000003; OWQ98293.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JZ38; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000197097; 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; 1.
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 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:UP000197097};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..254
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 349..447
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 450..741
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 791..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..811
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 91918 MW; F0A2336E509D53B3 CRC64;
MVADSPPDFR LRLRRDSNAV LGWFRDMWTR RWFRWLGYLA LSGLLGLFLI WLIFARDLPS
VDQLRDYEPP LPTMVRDAEG KPVHAYARER RVQLDYNEYP KTLVNAFLSA EDKTFFSHGG
IDYPGIASAI ITNVTSSGRP VGASTITQQV AKNLLLTNEL SYRRKVREAI LAMRIENALT
KEQILELYLN EIPLGRRSFG VQAAARAYFD KDVDQLALHE MAFLAILPKA PEKYGRARFV
DEALARRNFV LGSMASNGAI TAAQRDAARA MPLGLTDSGN RAVAQVGGYY MEEVRRQLIA
EFGETAEDGR LSVYAGGLWV RTPYDAKMQA AATNALRRGL IRYDAGKGWS GPIATIEADD
KWASRLASSF IGIDYDGWRI AAVVSKSPGA AQIGFADGTT GTLPAGAATL GYRKTGGSAF
SAMRPGDLIA VKATGGNSYA LKNIPEVSGG FIAESPHSGR IYAMQGGFDV RLSPFNRATQ
AERQPGSTIK PFVYATALDN GMTPATLIVD GPFCVYQGAN LGNKCFRNYG GAGGSGEHTM
RWGLEQSRNL MTVKTASQVG MEPIVETIQA MGMGKHEPYL STALGAGSTT VEKITNAYAM
LANHGRELKP RVIDYAQDRR GKVIFPKNWK PCDGCNKKDW DGRPMPRFAK SGKQLMDPMT
AYQVVHMLEG VVQRGTAVRL RDLGVPLFGK TGTTTGPNDV WFVGGTPNVV AGVYVGFDQP
RNMGGYAQGG SMAAPIFKQF FEESLADSQP VPFVAPKGVR MVRIDRQSGR RVYGSWPGSD
PKASIIWEAF KPESEPRRTI REEEIKPIKP ARRQDAPVQQ GPSRRTDSEF LEDRGGII
//
