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Database: UniProt
Entry: A0A1G4W099_9MICO
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Original site: A0A1G4W099_9MICO 
ID   A0A1G4W099_9MICO        Unreviewed;       849 AA.
AC   A0A1G4W099;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:SCX14734.1};
GN   ORFNames=SAMN05216534_1564 {ECO:0000313|EMBL:SCX14734.1};
OS   Candidatus Aquiluna sp. UB-MaderosW2red.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Aquiluna.
OX   NCBI_TaxID=1855377 {ECO:0000313|EMBL:SCX14734.1, ECO:0000313|Proteomes:UP000243284};
RN   [1] {ECO:0000313|Proteomes:UP000243284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UB-MaderosW2red {ECO:0000313|Proteomes:UP000243284};
RA   Varghese N., Submissions S.;
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; LT627734; SCX14734.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4W099; -.
DR   STRING; 1855377.SAMN05216534_1564; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000243284; Chromosome i.
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   CDD; cd06577; PASTA_pknB; 2.
DR   Gene3D; 3.30.10.20; -; 2.
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; IPR005543; PASTA_dom.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51178; PASTA; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:SCX14734.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243284}.
FT   DOMAIN          706..773
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
SQ   SEQUENCE   849 AA;  90555 MW;  6A4A019C26D60A6F CRC64;
     MSGKSKGSAL TTFLKFGLFS AVAGVLSVAL LAPAVAVAGV AASTGIGMFE GLPSYIRPVN
     SAESSTVYAL KNGVPVKMAT FFHENRVEVP FEDISPNLVN AVIATEDPRF YEHGGVDIIS
     LVRAALTNLA TFGDGPGAST ITMQYVRQSL VEAANLSGDA SAIAAATEVT IERKLREIRL
     SIALEQQFSK KDILAGYLNL VFLGNQINGV ETASQYYFGI SAKDLNIPQA AYLAAMLKSP
     NDYKPDEAAN LERGIGRRNY VLQQMADAGY ISFEQAESYK TSPIQTKITK TRQGCQENQV
     TAFFCDFTVW TIRNSPEFGV TPEEREILLR RGGLEIYTSL DLSVQQVAWD TTMEDLPPEN
     EWGFGTASVS VEVGTGRIIS MAQNRYFDQS TEPVLGGTSV NYNTDKNYGG SSGFQPGSTY
     KVFTLAQWLK DGHTLGEHVD GRIFTGEDVD LDGKPDPVKI WNVEKDFRAS CGGVAGLWEV
     NNSGDKTVDD ISVFQAVVTS QNTAFAAMAA QLDLCAIRDT AAAFGVHRAD GAELEYFPAS
     ILGTNEISPL AMAAAYAGIS NAGLYCSPVA IDKVLLRRTK EELPVPKTQC SQAVTPEIAA
     AMTQVMRSVV SGGTGAAANP GDGTPLAGKT GTTDRRIHTW MTGFSSKVAT ATWVGNVVGL
     TSQSSKSING RAVSTIRHSI WKEIMREVDK HYEGEAFPSP DPKYVIAPMV TVPEVTGFEL
     ESAKVQLVTA GLSMQVITRE VASSQPVGAI AYTTPEFGTP VPKGSIVKVF ISSGGKIVVP
     NIAGMDYTNA FATLQELGLT PSFPQPSQLS LNSRCDPIWP NDLAIGTSPA VGTEVSNASA
     ILVIPNKCG
//
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