ID A0A221P1X1_9ACTN Unreviewed; 462 AA.
AC A0A221P1X1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=DUF5136 domain-containing protein {ECO:0000313|EMBL:ASN26172.1};
GN ORFNames=LK07_21595 {ECO:0000313|EMBL:ASN26172.1};
OS Streptomyces pluripotens.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1355015 {ECO:0000313|EMBL:ASN26172.1, ECO:0000313|Proteomes:UP000031501};
RN [1] {ECO:0000313|EMBL:ASN26172.1, ECO:0000313|Proteomes:UP000031501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 137 {ECO:0000313|EMBL:ASN26172.1,
RC ECO:0000313|Proteomes:UP000031501};
RA Ser H.-L., Lee L.-H.;
RT "Genome sequence of Streptomyces pluripotens MUSC 137T.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP022433; ASN26172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A221P1X1; -.
DR STRING; 1355015.LK06_020440; -.
DR KEGG; splu:LK06_020440; -.
DR OrthoDB; 3663940at2; -.
DR Proteomes; UP000031501; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031501};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..347
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 47840 MW; A7CB05458459ECF3 CRC64;
MTQLHTPKAS RNQETGRLSF MGPVSPPAVR FRAGGATGGG TSRRAPGTFS TVPAPKNSVR
RSLLVASAAL SSLSVATSAA LAAPTPSSSP STTPPAHMST VGGVRLGQPG TQVNLAPGVP
VLPKGLTARS WIVADAESGD VLATHNAHWR LAPASTLKML FADTVLPRFP RGTRHKVVPS
DLAGMGAGSS VVGIAAGHTY TVHDLWLGVF LRSGNDAVHV LSSMNGGVGQ TVKDMQAHAD
DLQALDTHVV SPDGYDEPGQ VSSAYDLTLF ARSGLQKKDF RDYCSTVRAR FGSREIQNTN
RMLSGDTDVP VYRGIAGVKN GNTTHAGATF TGVAERNGRV LLVTVMNPGK HEHNEVYKET
ATLFDWGFQA AGKVKPVGEL VPPRSAVADA TAQPGPSAAG QAYGTGGSGS APAARATAGS
RSSGMGIALA ITGGLLVLLA AGAFLVNRRW PLPDLRRRRT PS
//