ID E7NVK1_TREPH Unreviewed; 380 AA.
AC E7NVK1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EFW37404.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:EFW37404.1};
GN ORFNames=HMPREF9554_02111 {ECO:0000313|EMBL:EFW37404.1};
OS Treponema phagedenis F0421.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=754027 {ECO:0000313|EMBL:EFW37404.1, ECO:0000313|Proteomes:UP000004157};
RN [1] {ECO:0000313|EMBL:EFW37404.1, ECO:0000313|Proteomes:UP000004157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0421 {ECO:0000313|EMBL:EFW37404.1,
RC ECO:0000313|Proteomes:UP000004157};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) 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:EFW37404.1}.
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DR EMBL; AEFH01000181; EFW37404.1; -; Genomic_DNA.
DR AlphaFoldDB; E7NVK1; -.
DR STRING; 162.TPHV1_70077; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_0_0_12; -.
DR Proteomes; UP000004157; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR036582; Mao_N_sf.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EFW37404.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 215..360
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 380 AA; 42830 MW; 3E92BFBA06432085 CRC64;
MNTLNIFLSA LKFFNIPSDN KKGRLQATVM NGDKRIKTVL YAIIFFVFTS AIFAEGDYVS
ALDTAEKLNT FLSWDPLSED FYFSKSGHRA QCRVGLPMML LSGKELVFIA PPKIINSVLS
ISKETAIRLE SFFGYSLEQP IYRIGAILID PGHGGKDPGT HGSYTENGKT IVVKEKDITL
KTSKELYELL KVRYPDKKIL MTRYDDSFPT LDERVEMANS VKLNKYEAIL YISVHANYSW
NSKASGFEVW YLPPEYRREV ISKDAVSKEI FPIVNSMLEE EFTMESIMIA QSILDGLDAS
IGKQSKKRGI MEQAWFVVRN AKMPSVLIEL GFVSNPTEVR LLNTPSYLKK CAEGIYNGLV
SFITHFEGSG GFTGEGRKKL
//
