ID E4HKX0_9ACTN Unreviewed; 456 AA.
AC E4HKX0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase/D-alanyl-D-alanine-endopeptidase {ECO:0000313|EMBL:EFS92217.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:EFS92217.1};
GN Name=dacB {ECO:0000313|EMBL:EFS92217.1};
GN ORFNames=HMPREF9607_01558 {ECO:0000313|EMBL:EFS92217.1};
OS Cutibacterium modestum HL044PA1.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium; Cutibacterium modestum.
OX NCBI_TaxID=765109 {ECO:0000313|EMBL:EFS92217.1, ECO:0000313|Proteomes:UP000003179};
RN [1] {ECO:0000313|EMBL:EFS92217.1, ECO:0000313|Proteomes:UP000003179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL044PA1 {ECO:0000313|EMBL:EFS92217.1,
RC ECO:0000313|Proteomes:UP000003179};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S13 family.
CC {ECO:0000256|ARBA:ARBA00006096}.
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:EFS92217.1}.
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DR EMBL; ADZU01000027; EFS92217.1; -; Genomic_DNA.
DR RefSeq; WP_002529074.1; NZ_GL383185.1.
DR AlphaFoldDB; E4HKX0; -.
DR GeneID; 73016532; -.
DR PATRIC; fig|765109.3.peg.1468; -.
DR HOGENOM; CLU_017692_0_1_11; -.
DR OrthoDB; 56883at2; -.
DR Proteomes; UP000003179; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 2.
DR PRINTS; PR00922; DADACBPTASE3.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EFS92217.1};
KW Hydrolase {ECO:0000313|EMBL:EFS92217.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EFS92217.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 456 AA; 47461 MW; B32A039040E99D75 CRC64;
MPAWVPVTVG VAVTVIVVFA VIVSSLRSGS PAGQIGGGIL PYHHDNTAQA VPGRGIVAAA
VPTTPSAKPV AAAIANRVKS AGAAPGVLGA DIMDAATGET LYQSGQDSFL TPASNLKVLT
AIALLDCTDA GHRYTTKVVA NGSALTLIGG GDPYLRSKPS TKQPEYPSVE DLAKRTAAAL
KKAGTTTVTV NFDDTLFTGP DWNKAWPVDN YFDEVTPITS LWVDEGMINN SPWDRSKTPA
VLATNTFIGS LRSAGITVNG SVTRHKADAS AKEIAAVQSL PVEDLVTRTL QESDNSAAEV
LSRQMALVSG KPGSFAGGSQ ALEEHLKNLG VWQDGAVVQD GSGLSKGNRI TASMLSRAWQ
KILSTPKLQP VANAVPVGRV SGTLHNRFSD PSTAAGRGVV HAKTGTLDGV ISMSGWLRDA
DGRILVASFI LNKTDIRARS WLDVVYSNLA GCGCTR
//
