ID G2Z9M0_LISIP Unreviewed; 427 AA.
AC G2Z9M0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Putative N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CBW85960.1};
GN OrderedLocusNames=LIV_1477 {ECO:0000313|EMBL:CBW85960.1};
OS Listeria ivanovii (strain ATCC BAA-678 / PAM 55).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=881621 {ECO:0000313|EMBL:CBW85960.1, ECO:0000313|Proteomes:UP000001286};
RN [1] {ECO:0000313|EMBL:CBW85960.1, ECO:0000313|Proteomes:UP000001286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-678 / PAM 55 {ECO:0000313|Proteomes:UP000001286};
RX PubMed=22072644; DOI=10.1128/JB.06120-11;
RA Buchrieser C., Rusniok C., Garrido P., Hain T., Scortti M., Lampidis R.,
RA Karst U., Chakraborty T., Cossart P., Kreft J., Vazquez-Boland J.A.,
RA Goebel W., Glaser P.;
RT "Complete genome sequence of the animal pathogen Listeria ivanovii, which
RT provides insights into host specificities and evolution of the genus
RT Listeria.";
RL J. Bacteriol. 193:6787-6788(2011).
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; FR687253; CBW85960.1; -; Genomic_DNA.
DR RefSeq; WP_014092883.1; NC_016011.1.
DR AlphaFoldDB; G2Z9M0; -.
DR GeneID; 57076458; -.
DR KEGG; liv:LIV_1477; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR eggNOG; COG4991; Bacteria.
DR HOGENOM; CLU_014322_1_0_9; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000001286; Chromosome.
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; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR017293; N-acetylmuramoyl-L-ala_amidase.
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; 3.
DR PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 3.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 3.
PE 3: Inferred from homology;
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 29..92
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 98..161
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 169..233
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 427 AA; 46019 MW; 1DD2DC1DD0C5D3D5 CRC64;
MKNKFIFITV VSILLIAAGI VTTIAMANAN SLVVKAEVLN VRSGPGLAYD VTSQVRKNEV
LRVVGEENQW YKVQLDNGNS GWVASWLVEN TDVSAASNSV AIVTSDGGLN VREKPNTSSN
SLGLLNNGDQ VTVTSQRDGW AQIQYQGKSA WVSSDYLDIR ESVTKVDDSD LQTVTIREDS
TNIRSDASRD SEVIEKANSG QSFAIQGVQG DWYQIRTTSG TNGYVANWVV DVSDKGQTTT
PKSKTTKLSE ATIVIDPGHG GNDPGAKGAG GTIEKEMTLK TAKNLKSKLE ASGAKVILTR
NSDEYVSLKS RTNKAAKNKA DVFVSLHFDS LEDSDSGVSG QTTYYYDNSD KSLAESINAS
LGKELPTSNR GARVGDYYVI RENSQPAVLL ELGYLSSAKD ERNINSASYR SKIADAVVDG
LSDYFSN
//
