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Database: UniProt
Entry: A0A1R1MFZ2_9GAMM
LinkDB: A0A1R1MFZ2_9GAMM
Original site: A0A1R1MFZ2_9GAMM 
ID   A0A1R1MFZ2_9GAMM        Unreviewed;       704 AA.
AC   A0A1R1MFZ2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Lytic murein transglycosylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BGP75_05960 {ECO:0000313|EMBL:OMH38732.1};
OS   Motiliproteus sp. MSK22-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Motiliproteus.
OX   NCBI_TaxID=1897630 {ECO:0000313|EMBL:OMH38732.1, ECO:0000313|Proteomes:UP000187359};
RN   [1] {ECO:0000313|EMBL:OMH38732.1, ECO:0000313|Proteomes:UP000187359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSK22-1 {ECO:0000313|EMBL:OMH38732.1,
RC   ECO:0000313|Proteomes:UP000187359};
RA   Nakajima Y., Yoshizawa S., Ogura Y., Hayashi T., Kogure K.;
RT   "Draft genome of Motiliproteus sp. strain MSK22-1.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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:OMH38732.1}.
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DR   EMBL; MIEQ01000025; OMH38732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1MFZ2; -.
DR   STRING; 1897630.BGP75_05960; -.
DR   OrthoDB; 92254at2; -.
DR   Proteomes; UP000187359; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.20.10; Bacterial muramidases; 1.
DR   Gene3D; 1.10.1240.20; Lytic transglycosylase, superhelical linker domain; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR037061; Lytic_TGlycoase_superhlx_L_sf.
DR   InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR   Pfam; PF01464; SLT; 1.
DR   Pfam; PF14718; SLT_L; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000187359};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          464..530
FT                   /note="Lytic transglycosylase superhelical linker"
FT                   /evidence="ECO:0000259|Pfam:PF14718"
FT   DOMAIN          542..654
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   704 AA;  81052 MW;  FF243B9DAB722849 CRC64;
     MQHQPQGVIR LVSAVSPKQI FGSLTRWRHK PLQQGLLIIL GLIQPCIGSS ALAKTSEVKA
     SVSSLSEIAP AAPKPDFNTT AISPQKLRQL RSDYKKARKA ITTRNTKQLQ ILMPALVDYP
     LYPYLHYSQI TSDLSKLNQK NYNDFMESYK DTPLPSRLES KWLSYLAKRK RWNNFLDNYP
     ANTSSTSRQC QRLWALHQTG KKKLAYSQVL PLWKVGRSQP KSCDKIFRNW IKAGHLKEQD
     AWQRFWLVLE NGNRSLARYV GDLIKDSAHR RMVTTAINLH KDPVKLAKLK LPSKTPGYTQ
     LVVTSLKRLV WKDPEQALQL WQKLEPTLTL NTEQKLKLRQ RLGLSMLKKY HPRSGYWLKQ
     LDPKIEDPKL IEWGLRFHLS NQDWEAVEKL IAQLSPEDKD KGRWRYWLGR AMESNGSKPK
     AIGIFTELSR ERSFYGFLAA DRIGQTYSLN NSSQPVDQKV ISQLSKLPAL NRARELFHHD
     QLLDARREWW KLSRQFSADQ HIQSAHIARR WGWYTQAIRA TIYARHWDDL RLRFPAPYSQ
     SISTNAQRFS IDIPWIFAVT RQESAFAADV RSPAGAVGLM QLMPATAKQT AKSINLRYKG
     SHQLKNPSTN IQLGSAYLSK MLERHQGNRV HATAAYNAGP HRVKGWLEKR GALPVDLWIE
     SIPFDETRQY VQNVLSYSVI YSDLLGQPKQ FLTPVEASKL PPIN
//
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