ID A0A0A0JVP8_9MICO Unreviewed; 818 AA.
AC A0A0A0JVP8;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KGN41268.1};
GN ORFNames=N801_08525 {ECO:0000313|EMBL:KGN41268.1};
OS Knoellia aerolata DSM 18566.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385519 {ECO:0000313|EMBL:KGN41268.1, ECO:0000313|Proteomes:UP000030013};
RN [1] {ECO:0000313|EMBL:KGN41268.1, ECO:0000313|Proteomes:UP000030013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18566 {ECO:0000313|EMBL:KGN41268.1,
RC ECO:0000313|Proteomes:UP000030013};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia aerolata.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:KGN41268.1}.
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DR EMBL; AVPL01000020; KGN41268.1; -; Genomic_DNA.
DR RefSeq; WP_035936708.1; NZ_AVPL01000020.1.
DR AlphaFoldDB; A0A0A0JVP8; -.
DR STRING; 1385519.N801_08525; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000030013; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 1.
PE 4: Predicted;
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:UP000030013};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 702..766
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 591..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..818
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 86939 MW; 011D581BA96929AD CRC64;
MDGRAHNLAH VLRLLTGLVV LSVLMGLLMA GLAIPAIGAG GSATKSGVKA FNDLPSEFSV
SPLAQQSRIL DASGKLIANP YDENRIIVPL KNISPWMQKA QIAIEDSRFY EHGGLDVRGF
TRAMVSNFQS GDVQGASTLT QQYVKITLQE NALRRDDKDA AKAAVAKTYT RKLQELKYAL
DVERNYTKEQ ILTGYLNLVY YGDQAYGVEA AAQNYFGISA SKLTLVQSAL LAGIVQQPTT
YNPVQNPKQS QTRRNAVLDR MQVLGMATAK DVAAAKKIPV ANMLGNRKPP KGVCQRSAEP
FFCAYMMEYL QKSPQMAVLG KTPAERLKNI NQGGLTITTT LDPKLQQATL RELTKAVPIG
NRSNLGAAST VIEPGTGKIL AMAQSTDFAK SQLNLNVDQR YGGSQFGYQF GSTAKTYALV
AALESGMPLD GTINAPSASP EDPHSFTRAE MKGRCNSDKD WSVENDYRSG GEMSLARATA
ESINTAFGQL VIDVGCKKVH ETMGRMGVHQ GDGKPIYDSV ASITLGAGTM TPMTIAASYA
TLAARGKYCE PTPIASITSA GGKPVAVPPT SCKQVVRADI ADGVNALLQG PLRDPRGTAR
GSWDESRPAA GKTGTTNNHN QSWFVGYTPQ RAASVWVGNV IVAKNARGDL TTLNGKCFGT
YGCKRSVFGG TIAGPVWGEI MKAATAGLPV VNFTPPSAAV RNGNYVPLPD VVGNSVGTAR
AKLEALGFTV RVGAMVDSQV DEGRVARTSP GARAPKGGVV TLLISRGYES TPTAPARTQP
RQTFTQPTTR VTTPVAPDPT PGVKPPKPPK PPKPPTRP
//
