ID A0A0M8YGY0_9PSEU Unreviewed; 1176 AA.
AC A0A0M8YGY0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Penicillin-binding protein transpeptidase domain-containing protein {ECO:0000259|Pfam:PF00905};
GN ORFNames=ADK67_14845 {ECO:0000313|EMBL:KOX27089.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX27089.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX27089.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX27089.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:KOX27089.1}.
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DR EMBL; LGED01000136; KOX27089.1; -; Genomic_DNA.
DR RefSeq; WP_053717013.1; NZ_LGED01000136.1.
DR AlphaFoldDB; A0A0M8YGY0; -.
DR STRING; 1415542.ADK67_14845; -.
DR PATRIC; fig|1415542.3.peg.3243; -.
DR OrthoDB; 3350718at2; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001182; FtsW/RodA.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 93..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 606..628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 856..1165
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 848..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1176 AA; 125182 MW; E3E889857B3B2BF9 CRC64;
MTEIVAALAL FFAGPTAWSR LVLLAGLVLA LVNSFRFLTG RESAVMAADG APPRHVHEGR
TRYLRGPDAA LYIPLALVLS GACVGVFRLA PWFLVCAGLL GGLVFLAAMR LRAEHGRRGE
DSVAGPVLAV LLSTAMLLLV GVVMAIRLVV VPDPSVGFAP SFTRDALEEV ARSVALPLLV
LAGLLFAERV VDSRRFADLL GKLPKRPSTV YPAGIAAVVL LFVAPIFYSE GENDADLTFF
GFATPEYGKV VYIWVLAVIL ARYAIGFQVR PGKLFANASW RRARRALATS KHVSYTFTIF
GAVGLVGLLK RDIGPTIPLF AATFTVVVFL LRLQVRSGAR LRDTLNSSRS LWFALGAVVL
VAIPVLQMPY VQTRQDAWHH PWTFNWSVGC APAPEGVVEP TDTPEGLVPC LETLDGASAG
KRSQIAQSMA AVADGGLWGR GLSDTLLGRL PAGSTDFILA VVWNKLGGVV IVLLAMLLAM
LAVALARCRT HLTRYTDADD PAAQRRIRAA RLFAAGLAGM LVAQFGFVLV TTLNLLPHSG
ITAPFLSRGG QSTLALTAGV LIAVWLLYRA DRPANPVPAN TPRAVVDHSP VPAGLRHGRF
RRVAPVGLIA MFLGSVLLAA TITVAPYGRY AEDRPFCLTQ DARVDPARCS TDRTANRRTS
AELRIDGRVQ YVRDRAEQVW RPVGEPALAF SDLAGLLRLH GASSSLAYAL DPILDGGSGT
SLRERVLPTP GGPRVGYADL TIDPELQKAT TEALRADADG EGPLAGGVVI VDARTGHVLT
ASSAPSALGW TKDAKSGEPD QGQVDSYLEN HQEYGPITGD RVDESDRDCH TLEWDGRCKK
WSLDKKPEDF EEESLTERRR YAPGTPDDKL PALDQNRALD RAYGLGSTFK VVVAAAYLKE
PGTTAQTKIP SPPTYKPRSG LPIKNHVDGP CRGTDAAGKI TLKQALVVSC NTAFVALAEQ
LGWAKIRDTA TALGFCALDG TTPENHAWLA GPAAGAASCV PANVDAEGME GIGNNTLGGG
RVVGTPLQMA TVMTALGNGG KVVQPTVVAA SADPFGRNER RYRGEARQVL TETQARELGE
ALAGVTQDDG GTAHLLRAGD HALRVKTGTH ELYGPDQDPP AGEFAKQVAW VVGALDTATG
PVAFAVAVET KDENAGSRRA RWLAQRVIDE VVEVRG
//
