ID B8JA70_ANAD2 Unreviewed; 603 AA.
AC B8JA70;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ACL65589.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:ACL65589.1};
DE Flags: Precursor;
GN OrderedLocusNames=A2cp1_2251 {ECO:0000313|EMBL:ACL65589.1};
OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL65589.1, ECO:0000313|Proteomes:UP000007089};
RN [1] {ECO:0000313|Proteomes:UP000007089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Beliaev A.S., Richardson P.;
RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001359; ACL65589.1; -; Genomic_DNA.
DR RefSeq; WP_012633426.1; NC_011891.1.
DR AlphaFoldDB; B8JA70; -.
DR KEGG; acp:A2cp1_2251; -.
DR HOGENOM; CLU_014322_11_0_7; -.
DR Proteomes; UP000007089; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACL65589.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..603
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002872654"
FT DOMAIN 438..590
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 26..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 64334 MW; 0D7E63E8E12AB3DF CRC64;
MRRAAVLLTV LMLAAPVEAA PAARYRGRTP AAAKHDAPRR TAARARPAPA PKKPAARAKV
SRLVDAKAAM SALMRDRNRR RYRHNWEKAI RGLEQAARGK DAPAALLEAS RARYALYRWS
AVEADRDEAL RLAARATRLG SRDAPALAAA IRREAGDDRP ARAAAPPRAA PKRAPTPAPA
APAAPEPEPA DADEEPAPEP ALDAALADLR GEPARPMPLG ESGGEGTATV SEVRAWSSGD
YTRVAIYLSH WVGWHKLELA PEGDRPRRLA LDLRPAHLDG KAVERAVAGD QVDRVRAAQN
GPDTVRVVLD LPGDDKVQLF TLDDPPRLIV DVGTHAAIHQ AIAGATRAPE PPPAPGPAAP
AGKAGPSAGE GELGPIRRIV VDAGHGGHDP GAIGPTRVRE KDVTLAIARR LARKLEAEGF
QVVLTRRDDR FLALEERTAL ANTARGDLFV SVHANAHPRR VRAGVETYFL NVADDRYAAR
LAARENGLDA EDAPSEVARI LSDLDAKASA DSSRRLAQLV QREVCAGVRS RVGDVKDLGV
KSALFYVLLG ARMPAVLVET GFISNRAEEQ RLGSARYQDE VASGITRAVA QFARGDARVA
AAR
//
