ID   A0A1G9E9F6_9ACTN        Unreviewed;       473 AA.
AC   A0A1G9E9F6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase / D-alanyl-D-alanine-endopeptidase (Penicillin-binding protein 4) {ECO:0000313|EMBL:SDK72718.1};
GN   ORFNames=SAMN05421874_110186 {ECO:0000313|EMBL:SDK72718.1};
OS   Nonomuraea maritima.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=683260 {ECO:0000313|EMBL:SDK72718.1, ECO:0000313|Proteomes:UP000198683};
RN   [1] {ECO:0000313|EMBL:SDK72718.1, ECO:0000313|Proteomes:UP000198683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5681 {ECO:0000313|EMBL:SDK72718.1,
RC   ECO:0000313|Proteomes:UP000198683};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; FNFB01000010; SDK72718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9E9F6; -.
DR   STRING; 683260.SAMN05421874_110186; -.
DR   OrthoDB; 56883at2; -.
DR   Proteomes; UP000198683; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 1.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SDK72718.1};
KW   Hydrolase {ECO:0000313|EMBL:SDK72718.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:SDK72718.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198683};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          39..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  48534 MW;  7FF155E2434023EC CRC64;
     MARRDRWVML TTLAVLQAVT VVIAVYAMMT GLTLDALTGS SPTSPAASSP AEGSSPVPVV
     TAGPVLARLT AKSGDGPLPT KSTLTRQLTD ALGDPALGDR VGAVVIDATT GERVFGSNPD
     LPVTPASTTK VVTCAAALAA LGPDTKLATR TVQGATPGSV VLVGGGDPML AGPYAKPTYP
     KQASLRTLAA RTAAALSAKG VRKVTLSYDS SLFVGQTKAD GWKTNYIPDG EVSPVHALAI
     DEGRQNPRMR APRVADPPQY AADAFAKLLA RRGIKVSGSV RPAKAAAGAA ELARVESAPL
     YALVEHTLTH SDNDFAEALL RHVAIKEGQE ASFAGGAKAV GAVLQRLGVT QPVKLSDGSG
     LSIRNRITPS TLAEVIAMTG SSQHPELHAL ASGMPIAGFT GTLGKSTRFA LPDSKGQVGL
     VRAKTGTLNN VNTLAGFATT KDGRLVTYAF MADKVPVTAE PVLDRLAAIV SRS
//