ID A0A0C1NFB4_9CYAN Unreviewed; 595 AA.
AC A0A0C1NFB4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KIE11486.1};
GN ORFNames=DA73_0217440 {ECO:0000313|EMBL:KIE11486.1}, DA73_0400013195
GN {ECO:0000313|EMBL:KAF3886326.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11486.1};
RN [1] {ECO:0000313|EMBL:KIE11486.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE11486.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3886326.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3886326.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:KIE11486.1}.
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DR EMBL; JHEG04000001; KAF3886326.1; -; Genomic_DNA.
DR EMBL; JHEG02000048; KIE11486.1; -; Genomic_DNA.
DR RefSeq; WP_038079562.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1NFB4; -.
DR STRING; 1479485.DA73_0217440; -.
DR OrthoDB; 9772024at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
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; PF08239; SH3_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000029738};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 226..284
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 474..586
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 595 AA; 65186 MW; 941C48060BBEB0FD CRC64;
MKSVLALVII SSIVVTSNIV LAQEQSLKIV YPPAKYQTSA RKVFFIGTAP SNGQVTINGK
PITRSKSGHF APSFPLELGE NTFNIRYQEQ EVQIKVTRVS SQPELLQGLV FAKDSLTPAV
DTAKLPGELI CFSAIAAPSA SVSVKLGNQT IPLLPQPQMS QLPPNSAALT GQNQPSVQTQ
TDKYAGCTTV TESGNMGQPE FQLTRDGKTI TQQSSGKITV LSPAQLEVVE VTADSGVART
GPSSDYSRLT PLPKGTQATI IGRQGEWLRL DYGAWINSKE TRVLKGAVPP STIIRSLGYR
KLSGMTEMVF PLQVPVPVSV QQSDRNFTLT LHHTTAQTDI IRLDDDPVIS RLDWQQLPAL
PQGGQGGVQY SFRLKSDRQW GYKLRYEGTS LILALRHPPK VREKKQQKPL TGIKILIDPG
HGGKESGASG PTGFLEKDVN LIVSKLLRDE LVKRGATVVM TREDDREVSL ADRVAAIDKE
EPTVAFSVHY NSLPDEGDAE NTQGVGTFWY HPQAHDLAIF MHNYIVRELG RPSYGVFWDN
LALTRPFSAP SVLLELGFMS NPNEFEWVTD SSEQKKLAKV VADGIVEWFA TDAKK
//
