ID Q10XH3_TRIEI Unreviewed; 636 AA.
AC Q10XH3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ABG53051.1};
GN OrderedLocusNames=Tery_4034 {ECO:0000313|EMBL:ABG53051.1};
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG53051.1};
RN [1] {ECO:0000313|EMBL:ABG53051.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG53051.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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; CP000393; ABG53051.1; -; Genomic_DNA.
DR AlphaFoldDB; Q10XH3; -.
DR STRING; 203124.Tery_4034; -.
DR KEGG; ter:Tery_4034; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_031959_0_0_3; -.
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; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR013783; Ig-like_fold.
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 SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ABG53051.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 266..325
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 517..629
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 636 AA; 70574 MW; 7468435AAFFF5571 CRC64;
MGNFNPLLMV IRKAINFQVF RKIISLSTLE LIIFLGLINI ISPNAMSQNY EDNNQLPQDS
KSRKKSLFIA YPSPNHKTTS DRIFLIGTAS PEAEVTVNGK LINERSRMGH FAPTFPLQIG
ENIFTVQHQN EEIILKITRN SNQPPLPVGV AFTQDSLTPI KDIARMPGEL ICFQAIAPPN
ANISVLLATQ TIPLFAQSQI VNLPGNLAVL TGDNQPFPSG GDYYQGCTKV ETPGELGQPE
FQLSLMGKTV TQKAPGKVSI LSPTTFEIAE VTVEEGVART GPSTTYSRLT PLPKGTKALI
TGKEGDYLRL DYGGWIKANE TRIFTDATPP RSVIRSAIAR QVQGATEIRF PLQVPVPVTV
EQGARYLSLT LHNTTAQTDT IRLDDDPLIE RLDWQPVLTS TVQNEQAVRY KFNLKTDQQW
GYKLQYVGTT LLLTLRHPPA VKSVISSATQ PLTGMKILID AGHGSENDLG AIGPTGYPEK
NVTLIISKLL QNELINRGAL VYMTRKAEED LYPKDRVEMI NQQVPDLALS VHYNALPDYG
DALKTQGIGT FWYHSQAHSL AIFLHNYLVE KLDRPSYGVF WNNLALTRPA IAPSVLLELG
FMINPYEFEW IMNSQEQQKL AKALADGIVE WVKKSQ
//
