ID A0A252E2D5_9NOSO Unreviewed; 731 AA.
AC A0A252E2D5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Tail length tape measure protein {ECO:0000313|EMBL:OUL33858.1};
GN ORFNames=BV372_15160 {ECO:0000313|EMBL:OUL33858.1};
OS Nostoc sp. T09.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1932621 {ECO:0000313|EMBL:OUL33858.1, ECO:0000313|Proteomes:UP000195076};
RN [1] {ECO:0000313|EMBL:OUL33858.1, ECO:0000313|Proteomes:UP000195076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T09 {ECO:0000313|EMBL:OUL33858.1};
RA Cruz-Morales P., Corona-Gomez J.A., Gutierrez-Garcia K.G., Barona-Gomez F.,
RA Cibrian-Jaramillo A.;
RT "Metagenomics of subcommunity co-cultures reveals the complexity of the
RT cycad coralloid root endophytic microbiome.";
RL Submitted (JAN-2017) 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:OUL33858.1}.
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DR EMBL; MTAV01000067; OUL33858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252E2D5; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000195076; 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; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; PF13174; TPR_6; 2.
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:UP000195076};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..731
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012535700"
FT DOMAIN 568..681
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 731 AA; 82114 MW; 7B39BC7D552FA666 CRC64;
MLKQLKKNPI PLIAGAGLCA FLAGAMVSAP EIGKSLGQWL KHGNNSPEQI SETSKAKSAV
YPLVSQSLPE RAAKLAEIAQ NPRSADRERA RYLLASDYIE RTQAKKALVL LEGLETDYPL
LAPYILLKQA QAQDLLGEDG KASDLRQKVL KQYPKTAAAV KAIYLIAQPK QQNLAIAQFP
SHPLTWEIIR KRLQENPNQP QLQLILAKYA ANQPGTVGVL DELAKGFTLK PEDWEIIGTA
YWTNNVFDKA GAAYAKAPKT PLNLYRTGRG LQVSGKNREK AIASYKQLVQ QFPEAQESGT
ALLRLAEMAK TRQEALPYLN QAIAKFPDAA SKALVEKAKI FQGLKDNKSA AQAWQLLIAK
YSNSDEAAEY RWKLAQEKAT AKDYAGAWQW AEPITTNNPT SILAPRAGFW VGKWATLLGK
QQEAKTAYEY VISQFPYSYY AWRSAAILGL NVGNFNTVRQ LKPEVVPPQR PVPTAGSETF
KELYLLGQDR DAWLQWETEF QNKDKPTVAE QFTEGLMQLA RGENKLGIDT ISKLEDRETP
EEQAEYEALS KQSIYWQARY PFPYLQEIEK WSTQRQLNPL LVTALIRQES RFEPKVKSIA
NATGLMQVLP STAKWIAPQI KVDSKTINLE DPNDNIMLGT WYLDHTHQQY NNNSLLAIAS
YNAGPGNVSK WLQTIPTQDP DEFVEKIPFD ETKNYVRQVL GNYWNYLRLY NPEISGLVGQ
YSTAHPKLPT Q
//
