ID A0A0E4C7T9_9FIRM Unreviewed; 807 AA.
AC A0A0E4C7T9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cell wall hydrolase/autolysin, catalytic {ECO:0000313|EMBL:CFX11613.1};
GN ORFNames=508 {ECO:0000313|EMBL:CFX11613.1};
OS Syntrophomonas zehnderi OL-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX11613.1, ECO:0000313|Proteomes:UP000045545};
RN [1] {ECO:0000313|EMBL:CFX11613.1, ECO:0000313|Proteomes:UP000045545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX11613.1,
RC ECO:0000313|Proteomes:UP000045545};
RA Murphy D.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; CGIH01000005; CFX11613.1; -; Genomic_DNA.
DR RefSeq; WP_052729550.1; NZ_CGIH01000005.1.
DR AlphaFoldDB; A0A0E4C7T9; -.
DR STRING; 690567.508; -.
DR OrthoDB; 9813450at2; -.
DR Proteomes; UP000045545; 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; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_sf.
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; PF07833; Cu_amine_oxidN1; 1.
DR Pfam; PF08239; SH3_3; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 3.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 3.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CFX11613.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000045545};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 39..101
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 111..175
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 317..381
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 178..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 87552 MW; E5B0AA5ED6027AF0 CRC64;
MLRSSQPSFN HPGRMGRMGL WTLTVFIILA LLLVPSAQAA PGKITGSVVN IRSGPGSGYD
VVGTLLIDTK VEVLQSGADW SKIRYSNIEG YVASQYISTG QTVTPPAVPN TPAKQVKVIN
GPINSRSGPN ASYDKVEILP DQAVYNVIGQ KDGWYQIQLS GGKTAYVAGW LVQEIGSSSP
APAPQPPTPA PPAGTGSHAV SSVLFNNQPL KFEVPPRIEN GRTLVPLRTI FEAMGAYVEW
NESTRTVIAR RGSTTVILPL GSTSPTVNGQ TWQLEVPAKI VNDRTLAPLR FVGEAFGGKV
AWNEQTRVVT IAYNPAPTPA VVAVKEGAVN LRENPSTTAA RAGVANAGER LNVLSEKNGW
YQVSQGGRTA WVASWVVEPA AGNSPEPVPV EPVIPPVVEP TPQPPAPPAP VPDPENALRL
SRSRDASGIK VVISSRQKLE PQIQESSGSI RYAFTNRPLL GLNYFEEKMG SELLKVKASD
YDKDTQITIS LPSEVEYKTM VEDGGKKLVL YIPNYLINIE KSPFGSVGER FVISTLCPVT
PAGKASGDRL EVTLPGLNLK KGINYNYSSD LVKSLQVEKN ANNLLMTFDI QGQYKHSFAV
SGSNNDLNII LMRKTTNQNR EKLVVLDAGH GGKDPGACGT LIKEKEVTLP VTLKVGELLK
QKGIPVEYTR TDDRFVELNE ISNIANRLNA TLFVSIHCNS STSPDPSGTE TYFYAPLTTP
ELYVQRDERQ KLATLLQNEL MSKLQRINRG VKEKNLAVLR NAQMPSALVE LAFISNPAEQ
ALLMQDDFQN LAAQAIANAI EQYMREM
//
