ID A0A1H4JYU1_9FLAO Unreviewed; 782 AA.
AC A0A1H4JYU1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN04489761_1135 {ECO:0000313|EMBL:SEB51186.1};
OS Tenacibaculum sp. MAR_2009_124.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250059 {ECO:0000313|EMBL:SEB51186.1, ECO:0000313|Proteomes:UP000199366};
RN [1] {ECO:0000313|EMBL:SEB51186.1, ECO:0000313|Proteomes:UP000199366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_124 {ECO:0000313|EMBL:SEB51186.1,
RC ECO:0000313|Proteomes:UP000199366};
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; FNSF01000001; SEB51186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4JYU1; -.
DR STRING; 1250059.SAMN04489761_1135; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000199366; 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 Reference proteome {ECO:0000313|Proteomes:UP000199366};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..223
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 301..444
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 689..776
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 782 AA; 89028 MW; 6F701960A73DE2DF CRC64;
MERIKNYAKR NKIKTILFVG LLIGYYFCLP KKLFTNPTST VVTSNNDELL GAVIASDGQW
RFPELDSIPS KFKHCILQFE DAHFYKHFGF NPVSIVKALK ENYKAKRVVR GGSTITQQVI
RLSRKNQRRS YFEKLVELIL ATRLEFRSSK EEILRLYASH APFGGNVVGL EMAAWRYFGL
HPYQLSWAES ATLAVLPNAP SLIYPGKNQE HLRVKRNTLL KKLFTEGIID QETYELATEE
ELPQKPYPLP TVASHFIQEV AKTKRGQRIK SSINIHLQKQ INTLAKQHYE QMKQNEVYNL
AVLVLDVETR KVLSYVGNSP TDGKHQKDVN NIVSPRSTGS TLKPFLYAQM LQEGALLPTQ
LVVDIPTEIA GYSPKNFDLT FDGAVPANEA LTRSLNIPAV RMLQSYGLEK FREDIKAYHI
KHINKSSDYY GLSLILGGAE ASLWDLCKTF AGYAGIVNHY EELRHEYYTN EFLEPSILHD
NELSFGAIKK EYTTIDAGTA YSTLNTLTEV NRPLTDQAWK YYDSSQKIAW KTGTSFGNKD
AWAIGATSKY VVGVWVGNSD GEGRSNLTGV GSAAPLMFNV FDVLPSSEWF LEPFEDLYEE
EICTKSGYLA LPICPSEKQK IPKNGRRADA CPYHKEIAID ITEKFRVNSN CESVSNIKTK
EWFVLPPLMA HYYQQKNADY RPLPSFRKDC LMSENNSMEF LFPTKYKSTV SLTKNSEGKI
NSLILKVTHQ NSNAKVYWYL DDTFIGITQD YHEQEIQPKP GVYTIKAIDN FGNERSCIIE
LR
//
