ID   M1ZEI2_NITG3            Unreviewed;       455 AA.
AC   M1ZEI2;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CCQ91986.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:CCQ91986.1};
GN   ORFNames=NITGR_910035 {ECO:0000313|EMBL:CCQ91986.1};
OS   Nitrospina gracilis (strain 3/211).
OC   Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC   Nitrospinales; Nitrospinaceae; Nitrospina.
OX   NCBI_TaxID=1266370 {ECO:0000313|EMBL:CCQ91986.1, ECO:0000313|Proteomes:UP000011704};
RN   [1] {ECO:0000313|EMBL:CCQ91986.1, ECO:0000313|Proteomes:UP000011704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3/211 {ECO:0000313|EMBL:CCQ91986.1,
RC   ECO:0000313|Proteomes:UP000011704};
RX   PubMed=23439773; DOI=10.3389/fmicb.2013.00027;
RA   Luecker S., Nowka B., Rattei T., Spieck E., and Daims H.;
RT   "The genome of Nitrospina gracilis illuminates the metabolism and evolution
RT   of the major marine nitrite oxidizer.";
RL   Front. Microbiol. 4:27-27(2013).
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:CCQ91986.1}.
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DR   EMBL; CAQJ01000101; CCQ91986.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1ZEI2; -.
DR   STRING; 1266370.NITGR_910035; -.
DR   HOGENOM; CLU_014322_11_0_0; -.
DR   InParanoid; M1ZEI2; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000011704; Unassembled WGS sequence.
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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CCQ91986.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011704}.
FT   DOMAIN          292..445
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          186..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  51005 MW;  776D584141BBF0E3 CRC64;
     MARQTFVMGR LGKVLQIAAV VCLMIVWLPG PALSKPSAAS PANSLYDNAK KAYYQLLENA
     QRVPNRDDWV SVIRLFEKVL VTYPQTELAY KAAFTVGRLY QKLGKKLDSE SDLREAGRYY
     SLLLKEYPEG HLNDDSLFHL ADLDMYRKDY QGARERLQSL LKMYPEGDRV EASRKELKRL
     VRLLTKAPTT EKTPNDPVEV SNKDSLTPEK PENLVPALET VETEKNKHVP LVVVDAGHGG
     KDHGAIGHHG LKEKEVNLNI SKEVAAILTK RYKFRVVLTR DDDRFIELAD RGKIANQKNA
     DLFVSIHANA APHKAAQGIE TYYLGSGSTE QARETAAREN GNLIYSVADD EVQQILASLI
     STTKINDSSR LASKVQKILH GNMVKRYRDV HDLGVKEGPF FVLHDTNMPS ILVEVGFVTN
     QREEKRLGSK AYQKALAEAI AHGIYEFLKE KAPSI
//