ID A0A0P7X723_9GAMM Unreviewed; 884 AA.
AC A0A0P7X723;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=mrcA {ECO:0000313|EMBL:KPQ02035.1};
GN ORFNames=HLUCCO02_05065 {ECO:0000313|EMBL:KPQ02035.1};
OS Idiomarinaceae bacterium HL-53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae.
OX NCBI_TaxID=1298881 {ECO:0000313|EMBL:KPQ02035.1, ECO:0000313|Proteomes:UP000053932};
RN [1] {ECO:0000313|EMBL:KPQ02035.1, ECO:0000313|Proteomes:UP000053932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-53 {ECO:0000313|EMBL:KPQ02035.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (AUG-2015) 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}.
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:KPQ02035.1}.
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DR EMBL; LIHO01000012; KPQ02035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7X723; -.
DR STRING; 1298881.Ga0003345_0868; -.
DR PATRIC; fig|1298881.4.peg.1721; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000053932; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..243
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 368..463
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 468..763
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT COILED 653..680
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 884 AA; 97984 MW; 55FC57B2F219939F CRC64;
MRFSLLGDLG LLFVLKFFKF LFISMFTMGF IGLCAVIGLY FYVKPELPSV ETLRDVTFQT
PMQVFSEDGK LIAQFGEKRR IPVTYDDLPQ DLIDAVLATE DSRFYDHLGV DPIGVLRAVR
VLITTGSARE GASTITMQVA RNFFLTRDRV LMRKIKETFI ALHIERLLSK EEILALYMNK
PGLGHRSFGV AAAAEVYYGR TLDELTLAEL ATIAGLFQAP SALNPISNPE RSVQRRRIVL
DRMLDMGYIT EAEYEEAYNA PVTARYHVPE VEFSAPYVAE MVRRDMVERF GEDVAYNSGM
RVYTTINSEM QQAAEAALRE NLHGYDERHG YRGAVSKLWG YSTREVSNLS VGGPITAPML
EAILANNGQP WPHDVIRLHL ERQPRYGRLI AAVVLSVQEQ TAEVMLRTGE IVTLPWEAMD
WARPFLDHDR QGPAPQTAAE ILTSGDQIWV REVNDELRLA QLPGPSSSVV SMNPRDGAIQ
AIVGGYSFNV SQYNRATQAK RQVGSTIKPF IYSAALDQGF TLSTLVNDAP ITQWNPSAGS
AWRPRNSPEQ YDGPIRLREA LARSKNVVSV RLVRAMGVDT VADYLPRFGF AANDLARNET
IALGSASFTP LEMSRAFAVF ANGGFLVEPY FIDKIESTEG ELIFKTEPAI GCSECEEAQA
TVAELEAEQA ERDNEDAAQV EIPEELLALA DVKLAPRVLS AQTAYLVSNA MQSSIWGGGS
WQHNTGWNGT AWRAQVFRNR NMSGKTGTTN DVKDAWFAGF VRGHVGVVWV GFDNLDAELG
RTTLNPNLGR QRQPIVASES GGTTALPAWV EYMRTALPLV ESGAQPLPEG IVSARVDTRT
GKLSNQSDHT SLFEYFKQGT APTEFSEGDR SSPLIFEDVE EGLF
//
