ID A7GXE0_CAMC5 Unreviewed; 491 AA.
AC A7GXE0;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EAU00797.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EAU00797.1};
GN Name=amiA {ECO:0000313|EMBL:EAU00797.1};
GN ORFNames=CCV52592_0486 {ECO:0000313|EMBL:EAU00797.1};
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105 {ECO:0000313|EMBL:EAU00797.1, ECO:0000313|Proteomes:UP000006380};
RN [1] {ECO:0000313|Proteomes:UP000006380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92 {ECO:0000313|Proteomes:UP000006380};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) 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; CP000767; EAU00797.1; -; Genomic_DNA.
DR RefSeq; WP_011992043.1; NC_009715.2.
DR AlphaFoldDB; A7GXE0; -.
DR STRING; 360105.CCV52592_0486; -.
DR KEGG; ccv:CCV52592_0486; -.
DR HOGENOM; CLU_014322_11_1_7; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000006380; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EAU00797.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006380};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..491
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002709747"
FT DOMAIN 330..485
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 89..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54094 MW; 5802649D3585A06E CRC64;
MTRIIFVVLM LAMSLFSANE AQIFSNFDRN FATSTKAQKS KFHNDIKQIY VQAIINNDKN
LKKQTLSRLI ISSKALGLDS SSYLNDLNEL NGAKPAKTNS PDTQTRQTQT PIKQTPSTRP
LYLLSATKNG DTLVLKFNQP LDTSKLKTSA LNQKNIYRNI MDIEGVLNGS SLTYKNFITQ
EVHIAQFDKN TIRIVFSDRA QKTIKANVIG DALVISSENF VSNEKINAPL TKQPVKTQQS
TPIPPAQAQP PKTPAAPTSQ PRPHHITGGK TIVIDPGHGG SDPGAISGKM QEKVAVLAVG
KKLGEILKKR GYKVYFTRSN DTFINLRTRT KYANDKMADL FVSIHANAAP NAVKAASMHG
IETFFLSPAR SERSKNAAAL ENKSDIEEMN YFSQQTFLNV LNREKIIASN KLGIDMQREL
LAQARKVYSA SDGGVREAPF WVLVGALMPA VLVEIGYITH PVEGKMLYDD AYQNALALGI
ANGVDSYFAK N
//
