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Database: UniProt
Entry: H3NH71_9LACT
LinkDB: H3NH71_9LACT
Original site: H3NH71_9LACT 
ID   H3NH71_9LACT            Unreviewed;       701 AA.
AC   H3NH71;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=HMPREF9708_00210 {ECO:0000313|EMBL:EHR38126.1};
OS   Facklamia languida CCUG 37842.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX   NCBI_TaxID=883113 {ECO:0000313|EMBL:EHR38126.1, ECO:0000313|Proteomes:UP000006190};
RN   [1] {ECO:0000313|EMBL:EHR38126.1, ECO:0000313|Proteomes:UP000006190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 37842 {ECO:0000313|EMBL:EHR38126.1,
RC   ECO:0000313|Proteomes:UP000006190};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Facklamia languida CCUG 37842.";
RL   Submitted (JAN-2012) 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};
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:EHR38126.1}.
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DR   EMBL; AGEG01000002; EHR38126.1; -; Genomic_DNA.
DR   RefSeq; WP_006308088.1; NZ_JH601133.1.
DR   AlphaFoldDB; H3NH71; -.
DR   STRING; 883113.HMPREF9708_00210; -.
DR   PATRIC; fig|883113.3.peg.209; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_2_9; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000006190; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 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:UP000006190};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..247
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          352..597
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   701 AA;  78364 MW;  375F2AEAAE8F05EB CRC64;
     MTRDIQNRND KRPHYFKGLK NLWRYYRGWK WLIFLSLTLA LILSSYLVLI AKTTDVETLI
     NSMQEKTRIY DYQDAESGTL LAQKGTYISL DQISNPLKTT VVATEDKRFY EHNGFDAKGI
     GRALIRLVIN RNTSGGGGST LTQQLAKNAF LSQDQTLQRK LKELFLALEL EKAYEKDQIL
     EMYLNNAYFG NGVWGVQDAA LKYFGVNASD LDWNQSMVLT GMLKGPSLYN PIDDYDAAVA
     RRNVIADILY QQGILSQADQ VALQQAPIHL MDSYIQTQQG HEYPFYYDAV INEANRLTDI
     PEADLMAKGY KIYTYLNPAF QSALNQSYQD TAYLFNDDLT GARPLVQSAS AVVDPHTGGV
     MAVYGARGDY TYRGFNRAVD MFRSPGSAIK PLAVYLPALE AGYRIHTMVP DVVQEYGPDH
     YRPENINRTT EASGELPLYL ALAQSKNTSA VYLMDQLGIE TAVKKLNQFG IDVPSKDRQL
     TLALGAFSTG VSPLQLASAY ATFANQGVRQ ESAFIRRIED ANGKVVYNQG RPSRHLIMTQ
     QVAADMTSMM LDTYGGYGTG YGYGPDYGLI AGKTGSTEVR DGSNQTRDRW MVGYTPDFAI
     ATWFGLDDVE SGNLDDIMPQ GSGQVFKVQT NYLMNQSAQT PFKETFASQM TEETNQGVQG
     AWFDKVQQAV GEWMQGAWQW LIQQTQPLQE ALDQVVKSFG G
//
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