ID A0A2V1HNT7_9MICO Unreviewed; 849 AA.
AC A0A2V1HNT7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:PVZ94175.1};
GN ORFNames=DDQ50_10550 {ECO:0000313|EMBL:PVZ94175.1};
OS Amnibacterium flavum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Amnibacterium.
OX NCBI_TaxID=2173173 {ECO:0000313|EMBL:PVZ94175.1, ECO:0000313|Proteomes:UP000244893};
RN [1] {ECO:0000313|EMBL:PVZ94175.1, ECO:0000313|Proteomes:UP000244893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8JJ-5 {ECO:0000313|EMBL:PVZ94175.1,
RC ECO:0000313|Proteomes:UP000244893};
RA Tuo L.;
RT "Amnibacterium sp. M8JJ-5, whole genome shotgun sequence.";
RL Submitted (MAY-2018) 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:PVZ94175.1}.
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DR EMBL; QEOP01000002; PVZ94175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1HNT7; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000244893; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000244893}.
FT DOMAIN 755..819
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 786..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 849 AA; 88568 MW; CB9B4E29AE079AD8 CRC64;
MCTLFASGRN RAPPRAALPT VWEEGSTPVP VSSIGGRLGG LLGFVGMSVA AGVLATVAVT
PAIALSGVAA SSTIGIFEDL PDYLEIQPLS QRTNVYATNP DGSTHLLAYF YNQNRIEVGP
DQVNGFVKNA AVAGEDPRYY DHGGVDLQGT VRAIVNTYIL GGSVQGGSSI TQQYVKNVNI
QNAIRNLTDQ AEITAAYEQA TATTESRKVQ EMKYAIGLEK RYTKDEVLMG YLNIAGFGGN
VYGIEAAANY YFGTTAADAS LPQAASLLAI VNNPERFRLD RPDDPDNGTA NAYAANQARR
DYILGSMLAE RMITQQEYDD AIAAPVEPNI VQPTAGCGYA GQAGFFCDYV RRAFTTDDFF
GATDDERLSA LLTSGYDVYT TLDMELQSVA ERAINDNVPM TLADFDIGAS VVTVEPGTGK
IRAMAQNKIY SEDPEVLAAD GRYTAVNYNA DYPMGGSRGF QPGSTYKIFT LLEWLKEGHS
LGETVDGRVR DWQGSTWRDS CVDGGSITVG ESYRPRNDEG DSPNSISALQ STVTSKNTGF
LAMANQLDLC GIRDTAASMG VHRADTGAVV DAATGEVGTG ELLKNPADTL GTNEVAPLQM
AGAFATIAAN GVYCEPVAIE RIVASDGTEV AVPPSECSQV LDPAVASTAA FALQSAFESG
TGASSSSRLS PSAPTFGKTG TTDDAYATWM SGATTKAATV SGVYNVTGFV NQREYRLGGE
QVAVKRHRIF PAVMSVANAK WGGDALPEPS QALVRGRQVT VPDTTGLTLD VATSVLVGAG
FTVRDGGARD SGLPAGTVVA TEPGGGASPG AEITVYTSNG SQSAPAPGQG QGQGQGGQTG
DGGGPGDSD
//
