ID A0A316B603_9MICO Unreviewed; 789 AA.
AC A0A316B603;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Membrane peptidoglycan carboxypeptidase {ECO:0000313|EMBL:PWJ66961.1};
GN ORFNames=B0H03_101420 {ECO:0000313|EMBL:PWJ66961.1};
OS Rathayibacter iranicus NCPPB 2253 = VKM Ac-1602.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1328868 {ECO:0000313|EMBL:PWJ66961.1, ECO:0000313|Proteomes:UP000245674};
RN [1] {ECO:0000313|EMBL:PWJ66961.1, ECO:0000313|Proteomes:UP000245674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1602 {ECO:0000313|EMBL:PWJ66961.1,
RC ECO:0000313|Proteomes:UP000245674};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PWJ66961.1}.
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DR EMBL; QGDV01000001; PWJ66961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316B603; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000245674; 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; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 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:PWJ66961.1}; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 713..780
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 745..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 789 AA; 82368 MW; DA1AEB768A0A10E7 CRC64;
MSGRGGTSVV KTIGGALAGF VGIVAMSVVA GVLVAASITP AIALSGMAAS DAVEMFDNLP
EYLEIGTLAE KSDVYAKDAS GGDVLLASFY AQNRVQVGWE EISPSVTDAV VASEDPRFYA
HGGIDLLGTV RAAATTAMGG DVQGGSSITQ QYVKNVLVQK AEALSDPIER DAAYREATET
TPERKIAEMR LAIGLEKEYP KNDILLGYLN IALFGGTVYG IEAAARYYFG ISAKDLSLAQ
SAALVAIVNN PEKFRFDRPN NPANPAADGY PQTLDRRNYI LSRMDLESKV TPEQAQAAAA
EPLAPAITEP STGCQTAGAA AFFCDYVTWV IKNDDAFGAS QDERDATFKR GGYKIYTSLD
SELQQAAVSA TDDWVPKSMA NINIGSATVS VEVGTGRILA MTQNKDYSND PSETGAHITG
INYNTDFGYG GSSGFQVGST YKVFTLAEWL QEGRSLGERV DGTRRAYTTF RDSCEADGVY
TGAEPWNPGN DEGGNGGVTT ALQATTGSIN TSFAAMAQQL DLCGIRNTAL AMGVHRADGT
ELQRIAPTIL GTNEIAPLTM ATAFAGFANR GTVCTPIAID RIVDRSGTDI APPASECTQG
LSEEVAATAG HALQQVVTSG TGAPSNPKNG IPHIGKTGTT DDALHTWMVG ASTEVATATW
VGNVSGFTSM RGFTLDGVNA GQVRHQIWPR IMRVADAKYG GSAFPTPSRS LTDAPQEAVP
QVTGQSPAAA TARLRSAGFT VRVDGTPIPC DRPAGSVAQT DPPAGARAAK GTAITLQISA
GRGDPPPEN
//
