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Database: UniProt
Entry: A0A1M6UGD0_9FIRM
LinkDB: A0A1M6UGD0_9FIRM
Original site: A0A1M6UGD0_9FIRM 
ID   A0A1M6UGD0_9FIRM        Unreviewed;       240 AA.
AC   A0A1M6UGD0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   ORFNames=SAMN02745243_03496 {ECO:0000313|EMBL:SHK68274.1};
OS   Hespellia stercorisuis DSM 15480.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Hespellia.
OX   NCBI_TaxID=1121950 {ECO:0000313|EMBL:SHK68274.1, ECO:0000313|Proteomes:UP000184301};
RN   [1] {ECO:0000313|EMBL:SHK68274.1, ECO:0000313|Proteomes:UP000184301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15480 {ECO:0000313|EMBL:SHK68274.1,
RC   ECO:0000313|Proteomes:UP000184301};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
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DR   EMBL; FQZY01000072; SHK68274.1; -; Genomic_DNA.
DR   RefSeq; WP_073112814.1; NZ_FQZY01000072.1.
DR   AlphaFoldDB; A0A1M6UGD0; -.
DR   STRING; 1121950.SAMN02745243_03496; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000184301; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
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; SSF53955; Lysozyme-like; 1.
PE   4: Predicted;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184301}.
FT   DOMAIN          54..221
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
SQ   SEQUENCE   240 AA;  26997 MW;  1AC466751A0F9109 CRC64;
     MRTIYHCIRK VFSRLLAVAI CAVLIVGVVF TVRGYEMYQS AVRETSVSER VSDIQNQENY
     VKYEELPQFY IDAVISVEDH RFDTHCGIDV IAIGRAALSD IKAGSFVEGG STITQQIAKN
     LFFSQKKEMT RKFAEVFAAL DLEKEYDKSE IFEIYVNTIY FGSDYYGIYD AAMGYYGKAP
     SDLTDYESAM LAGLPNAPSA YSPDTNMDLA VQRVRQVLDC MVKFDAVTQE QAEAVQESAE
//
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