ID   G2KPX9_MICAA            Unreviewed;      1103 AA.
AC   G2KPX9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   OrderedLocusNames=MICA_2039 {ECO:0000313|EMBL:AEP10347.1};
OS   Micavibrio aeruginosavorus (strain ARL-13).
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Micavibrio.
OX   NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP10347.1, ECO:0000313|Proteomes:UP000009286};
RN   [1] {ECO:0000313|EMBL:AEP10347.1, ECO:0000313|Proteomes:UP000009286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARL-13 {ECO:0000313|EMBL:AEP10347.1,
RC   ECO:0000313|Proteomes:UP000009286};
RX   PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA   Wang Z., Kadouri D., Wu M.;
RT   "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT   aeruginosavorus ARL-13.";
RL   BMC Genomics 12:453-453(2011).
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; CP002382; AEP10347.1; -; Genomic_DNA.
DR   RefSeq; WP_014103570.1; NC_016026.1.
DR   AlphaFoldDB; G2KPX9; -.
DR   STRING; 856793.MICA_2039; -.
DR   KEGG; mai:MICA_2039; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_012369_0_0_5; -.
DR   Proteomes; UP000009286; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF00912; Transgly; 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:ARBA00022670};
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:UP000009286};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          164..371
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1103 AA;  123758 MW;  FD40A290A8B061FB CRC64;
     MSVDHNNNDN QTNDSTANEG HTAPPLTPKK KSTFRKWMIG TVAGTAIVGT PAGLFGLYEV
     HESDLQSKYF NEIASGKRFT TKITDPLIFP PAKGPFDDRR GYSHFAAYDQ TLTARGKWER
     SFIAPWYDRN IHGIQLNLLE DEKQQAGATI TDYTGDTMYQ ARFPRNVYKT FDDVPKKLLN
     ALLFVENAEL LADHPDKQNP AVEWDRFAKA SFHQVLKKMG VASEYPGGST AAVQKEKYKY
     SGGGRTESPI DKLQQMASAT ARAYKDGVDT TEVRKDIALD YINSIPLSSY PGQGDVEGIG
     DGIALWFGRD FAELNHLLTK DESTMDDAEM AEAGQAFREA FYLALSIKKP SEYLLRTRGR
     DELNARVDNL LPRLAREGII SERMRDAALN AKLEFSKSED IKRKMAVPHN KTEMSLRIEM
     MNALGVKTGL YGLDRTDASA ITTVNKDASE AVTQFLHGLK DVENVRAAGL LGYPMLKETG
     LEDITYSFTL YEAGEKANYL RVQTDTYQGA LNLNEGSKLQ LGSTAKLRTL VTYLECMAYL
     HEQLSGKDVF ALEEAKDQYK DNLSRWAIDY LIAEKSKDEP NLSLRALLDA SMERRYSANP
     GETFFTGGGI HRFNNFKNDE NGRVPTVRET LQNSHNLPSV RIMRDIVNFT MEHKMDVPDD
     IFTNPDSPQR ARYLEQFINK EGKVFLYRAW NAQRDKSRDD IFTDLVNKRD NRAQYQIAAL
     YRMIFPEGSV EHMANRLHEI EYRQDNPDAS DDAVIEHMVA KSSDEKVMKK MQAMYTMYDP
     ERFVYEPWKR DPQSNKFNLN DLAFITKVHP LDLWLAHENT KTNTPLSWSD AYAAATASNA
     EGETVMKDIY SWLLKPHKME AQNKRLRIIL EEDAFSHIHK MWAKNGFSFE KMTPSLGSAL
     GDSGDTPAAL AEFSGIIVNG GIRKPSIRFT DMTLAPDTEE RERAYTRKPE ESVRVMPQEV
     ADVALETMQL IVRDGTGFRA GKVVLDDGRV LNVGGKTGTG DNRDKFFTAG GGMTSAEVKN
     RTATFVFEID DPVSGKRFFG SVLLYVDGPN AAKHKFTSAG PTQVLKNILV MLKPFLNEAC
     GVTAPAQTAA LDQKKNAPKA PAP
//