ID A0A1H0N3T9_9ACTN Unreviewed; 776 AA.
AC A0A1H0N3T9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:SDO87186.1};
GN ORFNames=SAMN05660199_02728 {ECO:0000313|EMBL:SDO87186.1};
OS Klenkia soli.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=1052260 {ECO:0000313|EMBL:SDO87186.1, ECO:0000313|Proteomes:UP000199088};
RN [1] {ECO:0000313|EMBL:SDO87186.1, ECO:0000313|Proteomes:UP000199088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45843 {ECO:0000313|EMBL:SDO87186.1,
RC ECO:0000313|Proteomes:UP000199088};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
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DR EMBL; FNIR01000008; SDO87186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0N3T9; -.
DR STRING; 1052260.SAMN05660199_02728; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000199088; 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 SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:SDO87186.1}; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..258
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 351..660
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 695..745
FT /note="PASTA"
FT /evidence="ECO:0000259|Pfam:PF03793"
FT REGION 725..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 80247 MW; 312FE08104D05989 CRC64;
MSETHAVSKI GTLFKLVATV VVAGALVAGM MLPFVGGSGL VARNSASLLD ALPVELTDQT
PNGNTVVLAA DGSPITNFYE NNRTPVTADQ ISDVMKQAIV DIEDSRFYEH NGLDVQGTLR
ALAANIAAGG VAEGGSTLTQ QLVKQTLLQT ADTPEEAEAA DEQTVGRKLR EARLALALEE
TYSKDEILTR YLNIAYFGAG AYGIQAAAQR YFSMNAIDLT LPQASVLAGL VQSPTDDDPL
AHPEAAQARR DVVLNRMHQL GHITDQELAD TTAQPIATAE GQPPARNCVA ASIGGFFCDY
LQRYLIGKLG MTQQQLDNGG YTIQTTLRPD IQASGDQAVL NTLPMGDPLV GTFTAVEPGT
GHLLAMSNNR QFCSDVNNPA CESVNYNEVA SRGAGSTYKV FTAAAALEQG FSQYYTITTA
VPYVSRVYKG GCTATGNRNP SSPYCVINAG TYPATLDLEQ ALVRSSNTYF LALEDALGSV
EAPVRMAERM GMHFDRSNQT PADTIIDENR GSFTLGPDAT SPLDLASAYS TLAAGGTQCD
PTPVIAITNR DGSPATLTDG TVINTADSCN PGAVPAGVAS TMNQIMIGDT TASYGTARRA
AIPGHQIAGK TGTAQGNVSV SFIGSTPSYT ASVMVWNSDG NESVGGFGGN KPAEIFNDAM
APILANEPAE EFPAADATVA NGNTALVPAC GSASDCQSAI TAAGLRYAGQ TDVDSAEPAG
TLVGTNPAQG SRVQQGGSVS VQVSNGSGYV APAPAPDPGT AVDPNAPDTN GDGQPG
//