ID E6SEW1_INTC7 Unreviewed; 898 AA.
AC E6SEW1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1 {ECO:0000313|EMBL:ADU47718.1};
GN OrderedLocusNames=Intca_1200 {ECO:0000313|EMBL:ADU47718.1};
OS Intrasporangium calvum (strain ATCC 23552 / DSM 43043 / JCM 3097 / NBRC
OS 12989 / 7 KIP).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=710696 {ECO:0000313|EMBL:ADU47718.1, ECO:0000313|Proteomes:UP000008914};
RN [1] {ECO:0000313|EMBL:ADU47718.1, ECO:0000313|Proteomes:UP000008914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23552 / DSM 43043 / JCM 3097 / NBRC 12989 / 7 KIP
RC {ECO:0000313|Proteomes:UP000008914};
RX PubMed=21304734; DOI=10.4056/sigs.1263355;
RA Del Rio T.G., Chertkov O., Yasawong M., Lucas S., Deshpande S., Cheng J.F.,
RA Detter C., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Pukall R., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Intrasporangium calvum type strain (7 KIP).";
RL Stand. Genomic Sci. 3:294-303(2010).
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP002343; ADU47718.1; -; Genomic_DNA.
DR AlphaFoldDB; E6SEW1; -.
DR STRING; 710696.Intca_1200; -.
DR KEGG; ica:Intca_1200; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_322327_0_0_11; -.
DR OrthoDB; 3663940at2; -.
DR Proteomes; UP000008914; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR InterPro; IPR038731; RgtA/B/C-like.
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 Pfam; PF13231; PMT_2; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ADU47718.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:ADU47718.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008914};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..898
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003209094"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 773..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..350
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT DOMAIN 573..709
FT /note="Glycosyltransferase RgtA/B/C/D-like"
FT /evidence="ECO:0000259|Pfam:PF13231"
FT REGION 55..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 208
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 898 AA; 93433 MW; 348C71799CC0913C CRC64;
MRSHAATMQR SLSTVGVVVT LALASPTAAI AALATRTPVA ATPTPRCEEW QTVTQVPVSG
STRPTRPSST ATPRPRTSPA CRNAPPAPFP HPAWDPPTVV GGPRLAATGL VADVPAGAHR
PPPVPDVSYV LADLDTGEVL AAKSPHAWLR PASTLKTLTA LALIPRLDPA RRVLATSEHE
AADGTRVGIL AGNRYPVSTL FDALLLSSAN DAAYLLADAA GGYEQTVSLM NETAVGLGAH
DTVAVDPSGL DEDGQHSSAY DLALIGRAAM RLPTFRSYVS KRDAAFPGGT NRATGTVYRS
FQIQNINELL GRYPGAIGIK PGRTNRAQHT FIGAATRAGR TLIVTQMGST TGDWKDTAAL
LDWGFANADV ASPVGVLVEP DAAPPPPVPA AAPPMPGTPP APSAAANPTA TLGSAQAAVP
EWPVTERTAV GVATWGVTAL AAAVGLGLLG LGLLVVARRH AGHRSRPSSR LRQGPTVHRL
PSAHAALLPA AHAALLPAAI GAAATLLFVR FTPPGQPYDE PAHWSNVLFY ARQHRMPVLG
EPGTQYEAQM GPGYYAPSAL IADVAGAGTG EAPFWAVRLA WVLLVPVLVV LTAQTAAALG
ATRHTRLSAA ALVAVNPLML AMGSTVQNDY LAIVVAAAAV LLGVRLLRRP TPSWWGHVLL
GALIGLAILV KVVAVALLAA ALLTQALRTD TTPRVRTAQA LAVTAGVVAA AGWWFVRNLA
LYGDLTGAQG IASLGVSFPP MRLTSAEQAV TWLGSMVSYL FVPVEYYRNA VNAPLALEAL
AVGAAVALVI LLARAARRRG APVLALPRRV RRDPVRLLIV SVLVMTVAAY LVYALAVAWI
AARLLFLAAP VGAVVIAMAA RDRTGRAIVA GLLTAFVIAD VWLLISLARL PRAEYWIF
//
