ID   A0A448HK52_9ACTO        Unreviewed;       675 AA.
AC   A0A448HK52;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:VEG30114.1};
GN   ORFNames=NCTC11636_02590 {ECO:0000313|EMBL:VEG30114.1};
OS   Actinomyces howellii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=52771 {ECO:0000313|EMBL:VEG30114.1, ECO:0000313|Proteomes:UP000266895};
RN   [1] {ECO:0000313|EMBL:VEG30114.1, ECO:0000313|Proteomes:UP000266895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11636 {ECO:0000313|EMBL:VEG30114.1,
RC   ECO:0000313|Proteomes:UP000266895};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; LR134350; VEG30114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448HK52; -.
DR   KEGG; ahw:NCTC11636_02590; -.
DR   OrthoDB; 3176960at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000266895; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF2; SLL0670 PROTEIN; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266895};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        208..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          555..672
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          1..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   675 AA;  68850 MW;  072BCAF3E6414BB0 CRC64;
     MRIEDLPSGP GRTGVDDTAC ATPSTGSPAS EPATVSSPYG QVTGTVRPSS RPAGPAPSTA
     ARSAATLLEE RRRGQTTQTT QTISTTAPGA GASPAAATPD RPETHEATGP DTEIAAPVAA
     PAAGTAEEGR SAPETELSEQ PEQPEPPEQI AVAPPERATV SAPTPQAAAE PAPVPAGATT
     SLAPAAADAS GAGGPDAGSR RRRRLWPLFL SAAALLLLGA VGAGGYAYAD HYADVAVPGS
     LVAGVDVSGM SRQEIVSVVQ DRADGATVTV SGDASASASL ADLGVTVDAG ATADAVLARG
     EGVVDRFRAL LGSSDTPVVV SSDPEVAQAY ATSLVPEDVV KAVNATVVLN AEGTGFEITP
     ASSGTSLDSS VLEDAADQAA SSLSDSSVEV TFESSPPAVS DEEAQAVADT ANSWVSQDVT
     ITAADSSGSY TADAATKASW VTVSTEGDTV PSVSLDPEKV SQWVSAQVEE VTVEPVTGVR
     NVNSQGAVVE TSVEAVAGES VTNADAIVQA ITEAVSTGTS YTGAFEMTTA EETWEDKVIA
     DGAENLVYQA APGEKWIDIN LANKTVTAYE GATVVRGPVS MVDGDALTPT VTGTYKVYLQ
     RETQTMEGDN ADGTRYRTEN VPWISYFHEG YALHGAPWRS SFGYSGSHGC INMPVEEAHW
     FYTWAQIGTT VVSHY
//