ID U1FBF6_9ACTN Unreviewed; 831 AA.
AC U1FBF6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Penicillin-binding protein (Transglycosylase/transpeptidase) {ECO:0000313|EMBL:ERF56888.1};
GN ORFNames=H641_04971 {ECO:0000313|EMBL:ERF56888.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF56888.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF56888.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF56888.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
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:ERF56888.1}.
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DR EMBL; AOSS01000174; ERF56888.1; -; Genomic_DNA.
DR AlphaFoldDB; U1FBF6; -.
DR PATRIC; fig|1160719.4.peg.951; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000016307; 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:UP000016307}.
FT DOMAIN 717..780
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 706..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 89610 MW; 401877041F0BAFAA CRC64;
MPSTRNRPAS SNRSRARIDR LEAQTQSSSR FSAFLKFCLA GILAGLLTAG FVVPFAALAS
TTARVSADSL QHLPAEFGSN PQPQRSQIFM ADGSVMATFF DENREYVPLD KISPVMRQAQ
IAIEDNRFYS HGAIDLRGTM RALVSNMGGA STQGGSTLTQ QYVKQARIEM AVSAGDEEGV
RSAQEQTVSR KLQELRYAIA LEHDLSKDQI LERYLNIAYY GDGAYGVEAA AKHYFGVTAD
KLDLGQAAML AGLVQNPVSY DPVNNPEAAI TRRNVVLTRM KSLGLVSEKD VQAAMKQGFN
RSRVTYPKTG CISSKYPFVC NYVYQSLLSS PNLGKTRAER EKLVKRGGLE IHTLIDPKAQ
DSAQQAVSNW VGPTDPVLGG VATIQPGTGL IMAMAQSRPE MGTKSGQTYY NYLAPLGLGG
FGGFQAGSTF KAYTLAAALE HGIPISKHYY AGSPMDFTGE TFQGCKGKVR SGPFSVSNST
GHSGTMGLRT AAAYSVNTYF VQLERDAGLC NVTKMAKKTG VELASGKDIV KEYGAIPSFT
LGTAYVTPLS MASSYATFAA RGVHCDPVIV KSIKNKDGQN LKVPDANCKR VMSTQVADGV
NEVLKGVMNG TGAPARIPGG YPQAGKTGTT DSNEAVWFTG YTPAVAGAAF IAADSSSEHF
RGREVRSIRG LHMSTGKYLK GSGGGDAGQI YRKAMAATLM GKPRTSFSEA TDEIQHGKKV
PVPSTSGMNY DEAKKALKDA GFDTRTKRVH SEKPEGTFLG ADPDGGKAPQ GSTIDLRVSS
GPRPTYQRRV PQRDRWQQWQ QQQQPEQQQQ DPWQQQQPAP AEPPSYTQQP R
//
