ID A0A1F8H8F6_9BACT Unreviewed; 763 AA.
AC A0A1F8H8F6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OGN33470.1};
GN ORFNames=A3G51_01740 {ECO:0000313|EMBL:OGN33470.1};
OS Candidatus Yanofskybacteria bacterium RIFCSPLOWO2_12_FULL_43_11b.
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1802710 {ECO:0000313|EMBL:OGN33470.1, ECO:0000313|Proteomes:UP000177745};
RN [1] {ECO:0000313|EMBL:OGN33470.1, ECO:0000313|Proteomes:UP000177745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGN33470.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MGKY01000016; OGN33470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8H8F6; -.
DR Proteomes; UP000177745; 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 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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..275
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 425..677
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 763 AA; 86540 MW; FD476243ABCE81F1 CRC64;
MKRLWSKSRE LLDFIPESLR TDYWIIVFKR RSWPKWVFLA LFLSLLAGTA SFGFGWWYMF
KYDGCFFNLG CLTDDKGQPL DLEKLARSEF KKASYVYAKN GEETGKYFEE IRDPVRLDEV
PKLLQNAFLA AEDKRFYQHS GIDITAIVSA AVGNGLRSRG INIWRRSGGA STITQQLARL
EFADEVSDFK TRAQTLSRKL KEARLAIRLE KRYSKKEIFG TYLNYIWLGH GAHGVVSGSM
RYWGKNIRKE PLSIREAAIL ASINKYPVLY DPVFHRPLEP KIDKNTAPEA AAKLQEEYEE
KLARETIRMA TAKDRYNFVL ERMRNNGSIS LKEYEENLFQ KDKNPNTEEL ARLSPWKNPA
YGYSNRLVKE MLLSWGYSDE DLLYYGGLRI YTTFDPVLQR IASEEFERHL AFLNQSKKPE
DRLNGAFVAI EVKTGNILAL SGGNDFNETQ YNRAMASRSP GSGFKPFTYA AAIEYLHKDF
FDQICNCPFA MRGGGGKTWA PQNFREENPV PYGYIPLSTG LIRSVNLPTL NLAREIGMKA
IVQLSNNMGV HGNPGMIRDS DGEIWFKKPG YEIKGGLVPL LPTAIGASDV NLIELANAYA
VFFRGGTYVR PTLVREIKSA YGDETIFRAE PPTGKIILSE STSNKILALM RAVTKIGTSK
ISMRGIEQQV ACKTGTSDGP RDVSMWCGTP ELVIAVRFGM DDYRIIELPE YMAKVSGQTD
MQVSGGWVAG PLVRRIVDRI YAERKKIEFS PAVEAELQRL LNQ
//
