ID U2FT84_9GAMM Unreviewed; 792 AA.
AC U2FT84;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=ponA {ECO:0000313|EMBL:ERJ17623.1};
GN ORFNames=SSPSH_003538 {ECO:0000313|EMBL:ERJ17623.1};
OS Salinisphaera shabanensis E1L3A.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1033802 {ECO:0000313|EMBL:ERJ17623.1, ECO:0000313|Proteomes:UP000006242};
RN [1] {ECO:0000313|EMBL:ERJ17623.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ17623.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=21705588; DOI=10.1128/JB.05459-11;
RA Antunes A., Alam I., Bajic V.B., Stingl U.;
RT "Genome sequence of Salinisphaera shabanensis, a gammaproteobacterium from
RT the harsh, variable environment of the brine-seawater interface of the
RT Shaban Deep in the Red Sea.";
RL J. Bacteriol. 193:4555-4556(2011).
RN [2] {ECO:0000313|EMBL:ERJ17623.1, ECO:0000313|Proteomes:UP000006242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E1L3A {ECO:0000313|EMBL:ERJ17623.1,
RC ECO:0000313|Proteomes:UP000006242};
RX PubMed=24324765;
RA Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA Bajic V.B.;
RT "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples from
RT the Red Sea Extremophiles.";
RL PLoS ONE 8:E82210-E82210(2013).
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:ERJ17623.1}.
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DR EMBL; AFNV02000032; ERJ17623.1; -; Genomic_DNA.
DR RefSeq; WP_006913013.1; NZ_AFNV02000032.1.
DR AlphaFoldDB; U2FT84; -.
DR STRING; 1033802.SSPSH_003538; -.
DR eggNOG; COG5009; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006242; 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 Glycosyltransferase {ECO:0000313|EMBL:ERJ17623.1};
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:UP000006242};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transferase {ECO:0000313|EMBL:ERJ17623.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT DOMAIN 63..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 323..425
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 427..689
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 750..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 86774 MW; 836A3AFF94984F48 CRC64;
MKAMPRAARI LVFLLAGLLS AATLAVLVVA GVYLYFGPQL PSAGDIGDPE LNEPLRVYTA
DRKLIGEFGL ERRLPRTYDE IPQPLVQAFV AAEDDRFFEH PGVDYQGIAR AAYVLATTGR
KTQGGSTITM QLARNLYLTN DRTYVRKIKE IILALRLESK LTKEQILEIY LNKIYLGNRA
YGVGAASEVY YHKPLKELTI AQMAMIAGLP KAPSRYNPMA NPERAVERRN YVLSRMHALG
EIDDDTYNSA REAPVTATAR VADDRYEADY VAEMVRQDMV ARFGDDAYTS GFDVTTTLDA
ERQRAANRAL RKALLAYDGR HEWHGPEDTL DSATLDDAKA LKNALEEMNV AGGLIPAVVT
DVARRSATLM TERYGEITLD AKQMSWLGGN DPASKLVSRG DVVRLAYTGS KDEAKAWTLA
EIPKVQGAMV ALDPHTGGIE ALAGGFDFSL SKYNRAVQAQ RQPGSSFKPF LYSAALAHGF
TTASLINDAP VVYDSPDLSD AWRPRNYSGR IYGPTRMREG LVHSRNLVSI RLLRSIGINA
AVEHIAKFGL PEDQIPRNLS MALGSASFSP LQMAQAYAVF ANDGFQVKPY YIAKIEDGRG
DVEFEAEPKV ACASTRNCPA LQNTGSKRDA SRLAERVIDA SNAWLVGDMM RDVVKRGTGR
RAMTLGRNDL SGKTGTTNDQ IDAWFVGFNA DLVGISWVGF DKLTPMGHSE TGGHAALPMW
IDFMRVALDG TPEAIPPRPG DLVAVSIDPD SGQRALEGGG MTEYFRPENV PSVEEARRSG
KNAPSNEVEQ LF
//
