ID   A0A1H3HMZ0_9ACTN        Unreviewed;       786 AA.
AC   A0A1H3HMZ0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:SDY16832.1};
GN   ORFNames=SAMN05661080_02563 {ECO:0000313|EMBL:SDY16832.1};
OS   Modestobacter sp. DSM 44400.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=1550230 {ECO:0000313|EMBL:SDY16832.1, ECO:0000313|Proteomes:UP000199500};
RN   [1] {ECO:0000313|EMBL:SDY16832.1, ECO:0000313|Proteomes:UP000199500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44400 {ECO:0000313|EMBL:SDY16832.1,
RC   ECO:0000313|Proteomes:UP000199500};
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; FNOZ01000017; SDY16832.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3HMZ0; -.
DR   STRING; 1550230.SAMN05661080_02563; -.
DR   OrthoDB; 3397599at2; -.
DR   Proteomes; UP000199500; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06577; PASTA_pknB; 1.
DR   Gene3D; 3.30.10.20; -; 1.
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; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
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:SDY16832.1}; 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:UP000199500};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          673..735
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          735..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..786
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  81586 MW;  12FC664C13F0A9B8 CRC64;
     MSDTARFRLG ALGKLVAMVV AAGVLVAAML FPWVGGTGLA ARNSASLLDA LPVELTDQTP
     NGNTKVLAAD GSLITEFYSN NRTPATADQI APIMKQAIVD IEDSRFYEHN GIDVQGTLRA
     LVTNVAAGGV EEGGSTLTQQ LVKQTLLQTA KTSEERQAAD AETVGRKLKE ARLALALEQT
     YSKDEILTRY LNIAYFGAGA YGIQAAAQTY FSVNAADLTL PQASVLAGLV QSPKFNPIAY
     PEAAQTRRNQ VLNRMHDLGH ITDQELADVS ASPIQTAAEG AKAPNGCSSA TIGGYFCDYL
     QTYLSQQLKI TKTRLENSGW TIQTTLRPDI QASGDQAVLN TLPMGGGNDL AGVFTAVQPG
     TGHVLAMSVN RRYGCSEYEC ESVNLNTTAS AGAGSTYKTF TAAAALAQGY GSHYTITTPQ
     PYTSKRYKNG GKPYTISNVG NNYPDTLDME KALVMSSNTY FVALEDALGT IEAPARMAAA
     MGMHFDQPNQ KSLDQIIAEN NGSFTLGPYA TSPLDLASAY STLAANGTRC APTPLVSILG
     SNGEPALKED GTPVYAGDQC TPEAIPAGVA TTLNQIMIGD TTQSFGTAKR AAIPGHQIAA
     KTGTSQDNNS ATFIGSTPDY TASVMVFNPK KQENVGGYGG NKPATIYHDA MAPILANEPA
     HDFPPADPVV VAGNRPTVPS CDSVDACQEA LTQAGYTTRT AQVTSAQSAG TFLGTSPRAG
     AAANPGQQVT IQVSNGRGRR RAPAPAPAPA PAPAPAPAPA PAPAPAPAPP AAPAPPPDTN
     GDGLPG
//