ID X7FCI6_9RHOB Unreviewed; 653 AA.
AC X7FCI6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Tail length tape measure protein {ECO:0000313|EMBL:ETX30458.1};
GN ORFNames=RISW2_12370 {ECO:0000313|EMBL:ETX30458.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX30458.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX30458.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX30458.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
CC -!- SIMILARITY: Belongs to the virb1 family.
CC {ECO:0000256|ARBA:ARBA00009387}.
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:ETX30458.1}.
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DR EMBL; JAME01000003; ETX30458.1; -; Genomic_DNA.
DR RefSeq; WP_043766138.1; NZ_JAME01000003.1.
DR AlphaFoldDB; X7FCI6; -.
DR STRING; 1449351.RISW2_12370; -.
DR PATRIC; fig|1449351.3.peg.510; -.
DR eggNOG; COG0741; Bacteria.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000023430; 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 InterPro; IPR023346; Lysozyme-like_dom_sf.
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 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:UP000023430};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..653
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004978146"
FT DOMAIN 490..592
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 653 AA; 71197 MW; 56CE823F2FDBEC3E CRC64;
MSRLTAWLTA LVLMFAPALS FAQEGRPLAR AMDAVRSGNW SAAMIEARGD GQPALDVILW
LYLREGLGDA RQVQDFVARN ADWPGMDYLR EKSEEAIVEA SHADVRAFFD TTPPQTGTGV
LSYARALENA GEIGAAEATV VLAWRTLALS SEEVSSFLSQ HGDLLADHHV ARLDMALWKG
WTANAQRMLS LVDEGHRRLA EARIALQDMS PGVDVKIAAV PEGLADDPGL ARDRFEWRVR
KGRDADAIAL LLDRSSGAAS LGEPWAWAER RRTLARERMR AGDIDTAYRI AATHHMAPNG
EYAYADLEWL AGYLALRFQN APGRAVEHFR RMQAAVATPI SLGRAGYWIG RAEEAMGNAE
AARAAYAEGG RFQTTFYGLL AAEKAGLAPD PALAGDETYP PWQDAAFTES SVFKAGILLM
AAGEADLAER FLTHLSESLD ATAIGQLGAM LEEMDKPHIQ VMLGKRAAQA GLEVHRPYYA
LPGFAAGGHP VPTELVLAIA RRESEFDPGV ISPVGARGLM QVMPGTAQDV SGWIGESYAL
SRLTSDPAYN LRLGAAYLEH LARRFDGNVV MMSAGYNAGP GRPIQWMERF GDPRQGEIDV
VDFIEFIPFR ETQNYVMRVA ESLPVYRARL GLDPHPVPFS EELVGSTLLP LGE
//
