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Database: UniProt
Entry: V4J3A5_9GAMM
LinkDB: V4J3A5_9GAMM
Original site: V4J3A5_9GAMM 
ID   V4J3A5_9GAMM            Unreviewed;       464 AA.
AC   V4J3A5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=N838_19325 {ECO:0000313|EMBL:ESQ10091.1};
OS   Thiohalocapsa sp. PB-PSB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiohalocapsa.
OX   NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ10091.1, ECO:0000313|Proteomes:UP000017935};
RN   [1] {ECO:0000313|EMBL:ESQ10091.1, ECO:0000313|Proteomes:UP000017935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA   Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA   Orphan V.J.;
RT   "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT   consortia of the Sippewissett salt marsh.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00001561};
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:ESQ10091.1}.
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DR   EMBL; AVFR01001207; ESQ10091.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4J3A5; -.
DR   PATRIC; fig|1385625.5.peg.7177; -.
DR   Proteomes; UP000017935; 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; 2.60.40.3500; -; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
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; PF11741; AMIN; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017935}.
SQ   SEQUENCE   464 AA;  50589 MW;  CBA2EBBF195F2F6E CRC64;
     MRTKIATVSK LFASLSGVIP QVIWLVFIFA LSPDLVQAGQ TVVHGARIWN APDHTRVVLD
     TAAPIRHRIF ALDKPDRLVV DLSDASLKGK LPDANPGDLL VSDLRSGVRD GDDLRVVVDL
     KQPVKVKSFE LEPSDAYGHR LVIDLSPKHR RRGRAADKMP KPSGDAVLAA AESSAAATSR
     HDRSAPSFLS VQPKRGGQRD VIIAVDAGHG GEDPGAIGRN GTREKDVTLA ISRKLAALID
     KQQGMRAVMI RDGDYFVPLR QRIAKARKRK ADLFVSIHAD AFTDPNVRGS SVYTLSNGGA
     TSEAAKWLAA RENRADLIGG VKLAERNEVL ASVLLDMTQN ATIEHSSIAA THVLEKLRSL
     GHVHQTRIQQ AGFAVLKSPD IPSMLVETAF ISNPSEERRL RSEHYQKKLA HSLLQGILDY
     FRDYPPPGTR FARQRGGVGD DTTSDSRVHQ DESTQSLLAL GLDF
//
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