ID A0A1E8FA28_9ALTE Unreviewed; 810 AA.
AC A0A1E8FA28;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:OFI32468.1};
GN ORFNames=BFC17_06880 {ECO:0000313|EMBL:OFI32468.1};
OS Alteromonas lipolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1856405 {ECO:0000313|EMBL:OFI32468.1, ECO:0000313|Proteomes:UP000176037};
RN [1] {ECO:0000313|EMBL:OFI32468.1, ECO:0000313|Proteomes:UP000176037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW12 {ECO:0000313|EMBL:OFI32468.1,
RC ECO:0000313|Proteomes:UP000176037};
RA Wu Y.-H., Cheng H., Xu X.-W.;
RT "Alteromonas lipolytica, a new species isolated from sea water.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OFI32468.1}.
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DR EMBL; MJIC01000017; OFI32468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E8FA28; -.
DR STRING; 1856405.BFC17_06880; -.
DR Proteomes; UP000176037; 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; cd06583; PGRP; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR43283:SF11; BETA-LACTAMASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43283; BETA-LACTAMASE-RELATED; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000176037}.
FT DOMAIN 20..180
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 810 AA; 89984 MW; 843D79C9FD2C885E CRC64;
MWLLCALLLT SCSSRRIVEM PSANYGDRVK SLVLHFTAID YAKSVDALVV EGGLSAHYLI
PESNDPSDPG GKPRIIRLVD ENKRAWHAGK SYWQGRHGLN DHSIGIEIVN VPECERDGGM
APSLAEHGSN RLCIFPDYDP AQIEVVIALV KDIIARHPDI EPTAVVGHAD IAFDRKNDPG
PRFPWFELYQ AGVGAWYDNE TLASYWKTFN EHPASIGLLQ SALHAYGYGV IETGIADTST
LNAISAFQMH FLPWHVTGEA DSRTAAAVFA LLDKYFPEQN QALLARYAKE QLNQTADSYP
QQQGQIDVIA PELAPSERVF VNDRYGFKSY AGRGELIIEA DQPTSAKISV NGELLSLDET
FDADSTYRYS LARRTRTGIN TLAIADVSPP SAQLHIQVPY PVLRDNTQAY KSQFSAVDAL
INQDIEQGFP GAVLVVVKNG KVIKRTAYGY QKRFDENEQP LSHPQPMRTD TLFDLASNTK
MFATTLALMH LVDSGKLDVT QPIQHYLPEY RGAGREARRV SDLLSHKSGY APSINFYDPE
NPLGERFYSQ SKQHTSELLI TQAPFDSGNG LNATYSDTNF MLLGLIVERI TGMPLDRYCE
EWLYQPLGLS KTLFNPLLKG HHKDEFAATE LRGNTRGGRI HFPHIREYTL QGEVHDEKAF
YAMEGVAGHA GLFSTANDLA VLAQMLLNGG GYGETHLFSS DVMNAFVKPD NRFWSYGLGW
RRAANGVNRW HFGPYASDQA FGHTGWTGTA TVIDPALDLA VILLTNARHS PIVEEVEDEL
QFTGKQFETG RYGSIVSLVY EAVLTNQTKN
//
