ID I4B1S6_TURPD Unreviewed; 863 AA.
AC I4B1S6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Penicillin-binding protein, 1A family {ECO:0000313|EMBL:AFM11233.1};
GN OrderedLocusNames=Turpa_0581 {ECO:0000313|EMBL:AFM11233.1};
OS Turneriella parva (strain ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H)
OS (Leptospira parva).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Turneriella.
OX NCBI_TaxID=869212 {ECO:0000313|EMBL:AFM11233.1, ECO:0000313|Proteomes:UP000006048};
RN [1] {ECO:0000313|EMBL:AFM11233.1, ECO:0000313|Proteomes:UP000006048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1111 / DSM 21527 / NCTC 11395 / H
RC {ECO:0000313|Proteomes:UP000006048};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of genome of Turneriella parva DSM 21527.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; CP002959; AFM11233.1; -; Genomic_DNA.
DR RefSeq; WP_014801751.1; NC_018020.1.
DR AlphaFoldDB; I4B1S6; -.
DR STRING; 869212.Turpa_0581; -.
DR KEGG; tpx:Turpa_0581; -.
DR PATRIC; fig|869212.3.peg.556; -.
DR HOGENOM; CLU_006354_2_4_12; -.
DR OrthoDB; 343702at2; -.
DR Proteomes; UP000006048; Chromosome.
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 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; 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; 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 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:UP000006048};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..247
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 431..695
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 834..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 95682 MW; B1D2CD915C4658F8 CRC64;
MAADVTEINP PLKTLPWWQK LEKISLYAFF LSAFFGGLFL GFLHFRIHSK TGDLDRLASF
RPTIPTRLYD QKGRLISELF RHQRKLVSLD EIPRPVIAAF LAIEDSNFYD HFGIDFKGIL
RASLKNLRAM RVVAGGSTIT QQLVKGLYTE SERTLYRKIY EAILALQVEK AFTKDEILEM
YFNQTYFGHG AYGISAAAQF YFDKPVSKLN FMEASILAAL PKSPHNYSPI RAPHDAYRKN
RVSLNRLVEV GYITKQEADT LYKTFWPVYW KKIVTTPPSK TIFGEKVNNA PYFTEHVRQE
LIALYGEDVV YSKGLQVYTT LDLDHQQAAE RAFLPQLEKM DPIARNYNRF MTGGIDGSLL
STYYALANIV PLPGIKREYS LRNDFRKKFK DETADAFELV SLAMPSQQVN DVSSEFMSAN
REFRGDLHVQ GAMLALDMKT GRYTAMIGGR EFKSSDQFNR ATMAKRQPGS AIKPFVYGAA
LEARAIHYGM GFIDSPIVNI QPNGEQWAPA NFDSGFTGYV LAYRALSASL NLVSVQIYDL
VGPDAIINYI SRLTKAPESR FQPNPALSLG ASELTPAEML LGYAIIGNKG QDIIPHAIIY
IADRDGNVTA HPENDVIQAL NYKRRTGQIQ VIEEGPAFIL RKMMENVVNS GTPTDAIRNR
AGYKGPGAGK TGTSNSFNDV WFGGYTTDMA AVVWAGMDNG NMTLGRGVSG GDVIAPVWGA
FMRDIYNARG KLAEPFDQTL PRTVRSGGVC KYTGKWPNAQ CDKPEDLTGT LIPEPITVNG
KRRGVGGETC NCHHAESKSF LDLLQADHNL ANEEVGRENN RAYSLVDGDR VQKLGQLGGD
LPVPPAPNGT APAPAPTNGA APP
//
