ID A9BAV2_PROM4 Unreviewed; 362 AA.
AC A9BAV2;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ABX08964.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:ABX08964.1};
GN Name=amiC {ECO:0000313|EMBL:ABX08964.1};
GN OrderedLocusNames=P9211_10331 {ECO:0000313|EMBL:ABX08964.1};
OS Prochlorococcus marinus (strain MIT 9211).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX08964.1, ECO:0000313|Proteomes:UP000000788};
RN [1] {ECO:0000313|EMBL:ABX08964.1, ECO:0000313|Proteomes:UP000000788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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DR EMBL; CP000878; ABX08964.1; -; Genomic_DNA.
DR RefSeq; WP_012195585.1; NC_009976.1.
DR AlphaFoldDB; A9BAV2; -.
DR STRING; 93059.P9211_10331; -.
DR KEGG; pmj:P9211_10331; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_0_3; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000000788; 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:ABX08964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000788};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..362
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002732660"
FT DOMAIN 244..356
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 362 AA; 40203 MW; 08538BE7E627A9E5 CRC64;
MNLQYSKPLN FLVFTGVFVS SIFLSLPSNA ASALAAWLIR DEGVLLFRTS KNAKLKAFFQ
SSSNGRGERV WVDFPGELLR PRTLLGSGPI KEIRLGKPMD GITRFVVEFN PYVDLNPYQL
RLKGIAPDKW EMRLPGLPTR GLKNIGEGSI HRTAVNEPRK YPANSSYKNI HFSNLPTVPK
NRFLVVIDPG HGGPDSGAIG IGGLRESEVV LEVSHHVASF LTKRGVKVVL TRKRDIDLDL
PPRVNMANRL RADAFVSIHA NASRGFKKHI NGLETYYFSG SRGFSLAKNI QNEILKAAPR
SPDRGVRKGR FFVIRRTNMP AALVEIGFVT GRADSQSLSQ ADHRKKVAFA ISKGILNYLK
ED
//
