ID A0A1M5FSJ4_9FLAO Unreviewed; 784 AA.
AC A0A1M5FSJ4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05444344_2069 {ECO:0000313|EMBL:SHF94389.1};
OS Tenacibaculum mesophilum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=104268 {ECO:0000313|EMBL:SHF94389.1, ECO:0000313|Proteomes:UP000183998};
RN [1] {ECO:0000313|EMBL:SHF94389.1, ECO:0000313|Proteomes:UP000183998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13764 {ECO:0000313|EMBL:SHF94389.1,
RC ECO:0000313|Proteomes:UP000183998};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVV01000003; SHF94389.1; -; Genomic_DNA.
DR RefSeq; WP_073183533.1; NZ_FQVV01000003.1.
DR AlphaFoldDB; A0A1M5FSJ4; -.
DR STRING; 104268.SAMN05444344_2069; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000183998; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 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 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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 58..223
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 300..556
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 690..777
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 784 AA; 89589 MW; 41DAAAC5A79AA966 CRC64;
MQTIFKWIQQ NKIKTIITAF VVIVYYFCLP KKLFEIPTST VVTAKNNKLL GAVIASDGQW
RFPELDSVPR KFEYCILQFE DAYFYKHFGF NPISIGKAMV ENIKAKRVVR GGSTLTQQVI
RLSRKNKERS YFEKLQELIL ATRLEFRHSK KEILNLYASH APYGGNVVGL EMASWRYFGL
KPHQLSWAET ATLAVLPNAP SLIYPGKNQQ KLKNKRNRLL QKLHEEGIID QITYDLAIEE
ELPQKPYPLP TVAPHFVQEV TKQYRGQRVK SSIDIHLQRQ VNNLVKQHYF RQKQNEVYNM
AVLVLDVKTR KVLSYVGNSP TDKAHQKDVN NIIAPRSTGS TLKPFLYAQM LQSGDLLPSQ
LVADVPTEIA GYSPKNFNLT FDGAVPANEA LTRSLNIPSV RMLQRYGLEK FREDLKAYHI
SDINKSADYY GLSLILGGAE ASLWDLCKTF AGYAGIVNHY EELKHKYYQN EFIEPSFLSE
RTPDFGKVQE DYITLDAGAT FLTLNTLIEV NRPYTDQAWK YYDSSQKIAW KTGTSFGNKD
AWAVGVTPKY VVGVWIGNSD GEGRPDLTGV GSAAPLMFNV FDVLPKSNWF LEPYEDLIEA
AICEKSGFLA KTICPLVITK RVQKSAMKAK SCPYHQEITV DISEKYRVNS NCESISNMIT
KPWFVLPPLM AYYYQQNNAD YRSLPKYRSD CNQLESNTMD FVFPAKLTSK ISLTRGENNK
LNPIILKLTH ANAEAKVYWY LNKQFIGITE QYHEQAVMPK KGVHTITVID DFGNELKRII
ELKN
//
